SitesBLAST
Comparing 6938368 FitnessBrowser__SB2B:6938368 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
6umdB Crystal structure of human gac in complex with inhibitor upgl00012
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/409 of 6umdB
- active site: S150 (= S63), K153 (= K66), Y278 (= Y189), Y330 (= Y240), V348 (= V258)
- binding 2-(pyridin-3-yl)-N-(5-{4-[(5-{[(pyridin-3-yl)acetyl]amino}-1,3,4-thiadiazol-2-yl)amino]piperidin-1-yl}-1,3,4-thiadiazol-2-yl)acetamide: R181 (≠ S94), K184 (≠ S97), L185 (= L98), F186 (≠ V99), L187 (≠ Q100), N188 (≠ V101), E189 (= E102), Y258 (≠ L171)
6ul9B Crystal structure of human gac in complex with inhibitor upgl00023
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/409 of 6ul9B
- active site: S150 (= S63), K153 (= K66), Y278 (= Y189), Y330 (= Y240), V348 (= V258)
- binding 2-phenyl-N-{5-[(1-{5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl}azetidin-3-yl)oxy]-1,3,4-thiadiazol-2-yl}acetamide: R181 (≠ S94), K184 (≠ S97), L185 (= L98), F186 (≠ V99), L187 (≠ Q100), N188 (≠ V101), E189 (= E102), Y258 (≠ L171)
6loxA Crystal structure of human glutaminase with macrocyclic inhibitor (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 93:383/407 of 6loxA
- active site: S148 (= S63), K151 (= K66), Y276 (= Y189), Y328 (= Y240), V346 (= V258)
- binding (E)-15,22-Dioxa-4,11-diaza-5(2,5)-thiadiazola-10(3,6)-pyridazina-1,14(1,3)-dibenzenacyclodocosaphan-18-ene-3,12-dione: K182 (≠ S97), L183 (= L98), F184 (≠ V99), L185 (≠ Q100), N186 (≠ V101), Y256 (≠ L171)
5fi7A Crystal structure of human gac in complex with inhibitor upgl_00015: 2-phenyl-~{n}-[5-[(3~{s})-3-[[5-(2-phenylethanoylamino)-1,3,4- thiadiazol-2-yl]oxy]pyrrolidin-1-yl]-1,3,4-thiadiazol-2-yl]ethanamide (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/410 of 5fi7A
- active site: S150 (= S63), K153 (= K66), Y278 (= Y189), Y330 (= Y240), V348 (= V258)
- binding 2-phenyl-~{N}-[5-[(3~{S})-3-[[5-(2-phenylethanoylamino)-1,3,4-thiadiazol-2-yl]oxy]pyrrolidin-1-yl]-1,3,4-thiadiazol-2-yl]ethanamide: K184 (≠ S97), L185 (= L98), F186 (≠ V99), L187 (≠ Q100), E189 (= E102), Y258 (≠ L171)
5fi6A Crystal structure of human gac in complex with inhibitor upgl_00011: 2-phenyl-~{n}-[5-[[(3~{s})-1-[5-(2-phenylethanoylamino)-1,3,4- thiadiazol-2-yl]pyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2- yl]ethanamide (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/410 of 5fi6A
- active site: S150 (= S63), K153 (= K66), Y278 (= Y189), Y330 (= Y240), V348 (= V258)
- binding 2-phenyl-~{N}-[5-[[(3~{S})-1-[5-(2-phenylethanoylamino)-1,3,4-thiadiazol-2-yl]pyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2-yl]ethanamide: R181 (≠ S94), F182 (= F95), K184 (≠ S97), L185 (= L98), F186 (≠ V99), L187 (≠ Q100), N188 (≠ V101), E189 (= E102), Y258 (≠ L171)
5fi2A Crystal structure of human gac in complex with inhibitor upgl_00009: 2-phenyl-~{n}-[5-[[(3~{r})-1-[5-(2-phenylethanoylamino)-1,3,4- thiadiazol- 2-yl]pyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2- yl]ethanamide (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/410 of 5fi2A
- active site: S150 (= S63), K153 (= K66), Y278 (= Y189), Y330 (= Y240), V348 (= V258)
- binding 2-phenyl-~{N}-[5-[[(3~{R})-1-[5-(2-phenylethanoylamino)-1,3,4-thiadiazol-2-yl]pyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2-yl]ethanamide: K184 (≠ S97), L185 (= L98), F186 (≠ V99), L187 (≠ Q100), Y258 (≠ L171)
8bsnA Human gls in complex with compound 27 (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 10:300/311 of 8bsnA
8jueA Crystal structure of glutaminasE C in complex with compound 11 (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 88:378/401 of 8jueA
5w2jB Crystal structure of dimeric form of mouse glutaminasE C (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 96:386/411 of 5w2jB
Sites not aligning to the query:
8jubA Crystal structure of glutaminasE C in complex with compound 27 (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 87:377/401 of 8jubA
4o7dA Crystal structure of human glutaminase in complex don (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 13:303/313 of 4o7dA
- active site: S68 (= S63), K71 (= K66), Y196 (= Y189), Y248 (= Y240), V266 (= V258)
- binding 5-oxo-l-norleucine: Y31 (= Y26), Q67 (= Q62), S68 (= S63), N117 (= N114), E163 (= E158), Y196 (= Y189), Y248 (= Y240), G265 (= G257), V266 (= V258)
8gwrB Near full length kidney type glutaminase in complex with 2,2-dimethyl- 2,3-dihydrobenzo[a] phenanthridin-4(1h)-one (ddp) (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 88:378/501 of 8gwrB
5uqeD Multidomain structure of human kidney-type glutaminase(kga/gls) (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/507 of 5uqeD
- active site: S150 (= S63), K153 (= K66), Y278 (= Y189), Y330 (= Y240), V348 (= V258)
- binding N,N'-[sulfanediylbis(ethane-2,1-diyl-1,3,4-thiadiazole-5,2-diyl)]bis(2-phenylacetamide): K184 (≠ S97), L185 (= L98), D191 (≠ E104), Y258 (≠ L171)
O94925 Glutaminase kidney isoform, mitochondrial; GLS; K-glutaminase; L-glutamine amidohydrolase; EC 3.5.1.2 from Homo sapiens (Human) (see 5 papers)
36% identity, 95% coverage: 7:295/304 of query aligns to 231:521/669 of O94925
- Y249 (= Y26) mutation to A: Loss of enzyme activity.
- S286 (= S63) binding ; mutation to A: Loss of enzyme activity.
- K289 (= K66) mutation to A: Loss of enzyme activity.
- P313 (= P90) to L: in GDPAG; loss of enzyme activity; dbSNP:rs1558973667
- F318 (= F95) mutation to Y: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with S-322.
- L321 (= L98) mutation to A: Decreased enzyme activity.
- F322 (≠ V99) mutation to S: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with Y-318.
- L323 (≠ Q100) mutation to A: Decreased enzyme activity.
- N335 (= N114) binding
- E381 (= E158) binding
- N388 (= N165) binding
- Y394 (≠ L171) mutation to A: Decreased enzyme activity.; mutation to L: No effect on catalytic activity. Loss of inhibition by BPTES.
- Y414 (= Y189) binding
- Y466 (= Y240) binding ; mutation to A: Loss of enzyme activity.
- S482 (= S256) to C: in CASGID; increased enzyme activity; dbSNP:rs1558986214
- V484 (= V258) binding
P13264 Glutaminase kidney isoform, mitochondrial; GLS; K-glutaminase; L-glutamine amidohydrolase; EC 3.5.1.2 from Rattus norvegicus (Rat) (see paper)
36% identity, 95% coverage: 7:295/304 of query aligns to 236:526/674 of P13264
Sites not aligning to the query:
D3Z7P3 Glutaminase kidney isoform, mitochondrial; GLS; EC 3.5.1.2 from Mus musculus (Mouse) (see 3 papers)
36% identity, 95% coverage: 7:295/304 of query aligns to 236:526/674 of D3Z7P3
- Y254 (= Y26) mutation to F: Increased enzyme activity in the absence of phosphate. No effect on stimulation of enzyme activity by phosphate.
- S291 (= S63) binding
- K316 (= K88) mutation to Q: Forms dimers with full, phosphate-independent activity; when associated with A-325 and K-391.
- G320 (= G92) mutation to P: Loss of enzyme activity.
- 320:327 (vs. 92:99, 50% identical) Highly mobile activation loop
- K325 (≠ S97) mutation to A: Constitutive enzyme activity that is fully active also in the absence phosphate. Forms oligomers with full, phosphate-independent activity; when associated with K-391. Forms dimers with full, phosphate-independent activity; when associated with Q-316 and K-391.
- N340 (= N114) binding
- E386 (= E158) binding
- D391 (≠ A163) mutation to K: Abolishes assembly of dimers into functional tetramers. Loss of enzyme activity. Forms oligomers with full, phosphate-independent activity; when associated with A-325. Forms dimers with full, phosphate-independent activity; when associated with Q-316 and A-325.
- N393 (= N165) binding
- F394 (≠ A166) mutation to S: Impairs tetramerization and promotes formation of homodimers. Impairs activation by phosphate.
- Y419 (= Y189) binding
- Y471 (= Y240) binding
- V489 (= V258) binding
Sites not aligning to the query:
- 202 K→E: Increased stimulation of enzyme activity by phosphate.
- 207 K→E: Increased stimulation of enzyme activity by phosphate.
6umfA Crystal structure of human gac in complex with inhibitor upgl00012
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/409 of 6umfA
- active site: S150 (= S63), K153 (= K66), Y278 (= Y189), Y330 (= Y240), V348 (= V258)
- binding N-(5-{[1-(5-amino-1,3,4-thiadiazol-2-yl)piperidin-4-yl]oxy}-1,3,4-thiadiazol-2-yl)-2-phenylacetamide: L185 (= L98), L187 (≠ Q100), Y258 (≠ L171)
6uljA Crystal structure of human gac in complex with inhibitor upgl00012
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/409 of 6uljA
6ulaA Crystal structure of human gac in complex with inhibitor upgl00012
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/409 of 6ulaA
- active site: S150 (= S63), K153 (= K66), Y278 (= Y189), Y330 (= Y240), V348 (= V258)
- binding 2-cyclopropyl-N-{5-[4-({5-[(cyclopropylacetyl)amino]-1,3,4-thiadiazol-2-yl}oxy)piperidin-1-yl]-1,3,4-thiadiazol-2-yl}acetamide: K184 (≠ S97), L185 (= L98), F186 (≠ V99), L187 (≠ Q100), N188 (≠ V101), Y258 (≠ L171)
6ukbA Crystal structure of human gac in complex with inhibitor upgl00012
36% identity, 95% coverage: 7:295/304 of query aligns to 95:385/409 of 6ukbA
- active site: S150 (= S63), K153 (= K66), Y278 (= Y189), Y330 (= Y240), V348 (= V258)
- binding N-[5-(4-{[5-(acetylamino)-1,3,4-thiadiazol-2-yl]oxy}piperidin-1-yl)-1,3,4-thiadiazol-2-yl]acetamide: K184 (≠ S97), L185 (= L98), F186 (≠ V99), L187 (≠ Q100), Y258 (≠ L171)
Query Sequence
>6938368 FitnessBrowser__SB2B:6938368
MLEQALLDDLVAKVRPLLGQGKVADYIPALARVSPYKLGIAVTTIDGTTLGAGDWQEAFS
IQSISKVFSLTGAMMLYEEREIWSRVGKEPSGHSFNSLVQVELERGIPRNPFINAGALVI
ADLLQSRLGAPKQRMLEIVRMLSQNHKVCYDKVVADSEYQHSARNAAIAFLMKSFGNFHN
DVDKVLRSYFHYCSLSMSCADLSRAMVYLANQGVSLDGNEVVSPTQTRRLNALLATSGLY
DGAGEFAYRVGMPGKSGVGGGIIAVIPGDMSVCVWSPALDASGNSLAGTRLLELLAQELG
RSIF
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory