SitesBLAST

7tl8A 1.95a resolution structure of independent phosphoglycerate mutase from s. Aureus in complex with a macrocyclic peptide inhibitor (sa-d3) (see paper)
33% identity, 19% coverage: 287:363/402 of query aligns to 370:453/488 of 7tl8A

query
sites
7tl8A

D

D

F

L

L

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Y

I

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L

H

N

V

F

E

A

A

N

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D
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binding manganese (ii) ion: D380 (= D297), H384 (= H301), D421 (= D329), H422 (= H330), H439 (= H349)

Sites not aligning to the query:

binding manganese (ii) ion: 12, 62
binding : 61, 63, 64, 67, 77, 78, 120, 121, 189, 249, 252, 273, 315, 320

4nwxA Crystal structure of phosphoglycerate mutase from staphylococcus aureus in 2-phosphoglyceric acid bound form (see paper)
33% identity, 19% coverage: 287:363/402 of query aligns to 385:468/503 of 4nwxA

query
sites
4nwxA

D

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active site: D395 (= D297), H399 (= H301), D436 (= D329), H437 (= H330), H454 (= H349)
binding manganese (ii) ion: D395 (= D297), H399 (= H301), D436 (= D329), H437 (= H330), H454 (= H349)

Sites not aligning to the query:

active site: 10, 60, 152, 255, 328
binding 2-phosphoglyceric acid: 121, 152, 183, 189, 255, 258
binding manganese (ii) ion: 10, 60

4nwjA Crystal structure of phosphopglycerate mutase from staphylococcus aureus in 3-phosphoglyceric acid bound form. (see paper)
33% identity, 19% coverage: 287:363/402 of query aligns to 386:469/504 of 4nwjA

query
sites
4nwjA

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active site: D396 (= D297), H400 (= H301), D437 (= D329), H438 (= H330), H455 (= H349)
binding manganese (ii) ion: D396 (= D297), H400 (= H301), D437 (= D329), H438 (= H330), H455 (= H349)

Sites not aligning to the query:

active site: 11, 61, 153, 256, 329
binding manganese (ii) ion: 11, 61

1o98A 1.4a crystal structure of phosphoglycerate mutase from bacillus stearothermophilus complexed with 2-phosphoglycerate (see paper)
30% identity, 20% coverage: 284:363/402 of query aligns to 389:475/509 of 1o98A

query
sites
1o98A

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active site: D402 (= D297), H406 (= H301), D443 (= D339), H444 (= H340), H461 (= H349)
binding 2-phosphoglyceric acid: D402 (= D297), H461 (= H349)
binding manganese (ii) ion: D402 (= D297), H406 (= H301), D443 (= D339), H444 (= H340), H461 (= H349)

Sites not aligning to the query:

active site: 11, 61, 153, 260, 335
binding 2-phosphoglyceric acid: 61, 122, 152, 153, 184, 190, 260, 263, 335
binding manganese (ii) ion: 11, 61

Q9X519 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; 23PGA-independent; BPG-independent PGAM; Phosphoglyceromutase; iPGM; EC 5.4.2.12 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 4 papers)
30% identity, 20% coverage: 284:363/402 of query aligns to 390:476/511 of Q9X519

query
sites
Q9X519

E

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D403 (= D297) binding
H407 (= H301) binding ; mutation to N: Loss of mutase activity.
D444 (= D339) binding
H445 (= H340) binding ; mutation to N: 5-fold decrease in the mutase activity.
H462 (= H349) binding ; mutation to N: Strong decrease in the mutase activity.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
12 binding ; D→N: Loss of mutase activity.
42 H→N: Decrease in activity.
62 active site, Phosphoserine intermediate; binding ; S→A: Loss of mutase activity.
66 H→N: Strong decrease in the mutase activity.
123 binding ; H→N: Strong decrease in the mutase activity.
125 H→N: Decrease in activity.
128 H→N: 5-fold decrease in activity.
153:154 binding
185 binding
191 binding
261 R→L: Loss of mutase activity.
261:264 binding
336 binding

1ejjA Crystal structural analysis of phosphoglycerate mutase cocrystallized with 3-phosphoglycerate (see paper)
30% identity, 20% coverage: 284:363/402 of query aligns to 388:474/508 of 1ejjA

query
sites
1ejjA

E

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active site: D401 (= D297), H405 (= H301), D442 (= D339), H443 (= H340), H460 (= H349)
binding 3-phosphoglyceric acid: D401 (= D297), H460 (= H349)
binding manganese (ii) ion: D401 (= D297), H405 (= H301), D442 (= D339), H443 (= H340), H460 (= H349)

Sites not aligning to the query:

active site: 10, 60, 152, 259, 334
binding 3-phosphoglyceric acid: 60, 121, 152, 183, 189, 259, 262, 334
binding manganese (ii) ion: 10, 60

Query Sequence

>WP_010876057.1 NCBI__GCF_000008645.1:WP_010876057.1
MITMKHVILVGDGMADYPLDELDGKTPLQVADKPNMDQLAGMGACGLLRTVPEGMEAGSD
VANLSIMGYDPRRYYTGRGPLEAASIGVELGDDDVAFRCNLINADERIVDFNAGHIETAE
ASSLIDALNHELETRGRFYAGVSYRNLFVIEGRGYTSVRVEPPHDIVGESVAAHLPSGSE
EADHIRELMLESAGVLRSHEVNLKRESMGKRPATMIWLWGQGLRPSMEPFSERYGIRGAT
ITAVDLIKGLGVYAGLENIHVPGATGYLDTDYRAKGRYAAGALEEYDFLYVHVEAPDEAG
HAGDAEEKIRAIENIDRFVLGRLLDALSDHEHRIAVLPDHPTPIEIRTHVPDPVPCILAG
DGVDADQVKSYDEFTVREGSLGTWEAHRLMEIMMDPAARLRQ

Or try a new SitesBLAST search

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