SitesBLAST

1 modified: Initiator methionine, Removed
43 binding [2Fe-2S] cluster
48 binding [2Fe-2S] cluster
51 binding [2Fe-2S] cluster
73 binding [2Fe-2S] cluster
113 binding [2Fe-2S] cluster
116 binding [2Fe-2S] cluster
148 binding [2Fe-2S] cluster
150 binding [2Fe-2S] cluster
257:264 binding FAD
335 R→A: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents.
336 W→A: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents.
337 binding FAD
347:351 binding FAD
360 binding FAD
404 binding FAD
422 binding FAD
427 R→Q: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents.

3unaA Crystal structure of bovine milk xanthine dehydrogenase with NAD bound (see paper)
27% identity, 81% coverage: 166:904/907 of query aligns to 521:1270/1286 of 3unaA

query
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3unaA

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A

active site: Q729 (≠ I390), E764 (≠ F425), R842 (= R501), H846 (≠ F505), R874 (= R533), G1222 (= G868), E1223 (= E869)
binding calcium ion: A829 (≠ H488), S832 (≠ Y491), R833 (≠ S492), S836 (≠ G495), S869 (≠ W528), N870 (≠ G529)
binding carbonate ion: R801 (= R460), H802 (≠ S461), T871 (≠ S530), A872 (= A531), F876 (≠ Y535), G877 (= G536), Q880 (= Q539)
binding fe2/s2 (inorganic) cluster: L706 (≠ M368)

Sites not aligning to the query:

binding flavin-adenine dinucleotide: 43, 44, 227, 228, 229, 230, 231, 232, 233, 234, 307, 308, 316, 317, 320, 321, 323, 324, 329, 330, 373, 374
binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 110, 111, 112, 114, 146, 148
binding nicotinamide-adenine-dinucleotide: 327, 363, 364, 430, 431, 471, 478

Query Sequence

>WP_054029547.1 NCBI__GCF_001293685.1:WP_054029547.1
MMKRTLHVNGVPRTVIVEADQSLANVLREQLGLTGTKIGCGQAQCGCCNVILDDKLVRSC
VTKMSKVADGSTVITVEGIGNRDNLHPIQLSWIVHGGAQCGFCTPGFIVSVKALLDQNPN
PTREDVREWFQTHRNACRCTGYKQLVDAVMDAAKVMRGEMKAEDLLFRIPPDGHIWGTNH
PRPSAVAKVTGTLDYGADLGLKMPADTLYLALVQAKVSHANIKGIDTSEAEKMPGVFKVV
TAKDVTGKNRITGLITFPTNKGDGWDRPILCDQKVFQYGDAIAIVCADNEYQARRAAEKV
KVDLEELPAYMSAPAAMAEDAMEIHPGTPNVYFELPVVKGGETAPLMQSAAYTAEGDYYL
QRQPHLTMETDVGCAYFDDEERLTIHSKSIAIHLHSAMIAAGVGISPNKLRLVQNPAGGT
FGYKFSPTMEALLGVACMATGRPVFLRYDYQQHITYTGKRSPFWMKVKYGADKEGKIVAM
ESDWSVDHGPYSEFGDLLTLRGAQFIGAGYGIPNIRGMGRTVCTNHAWGSAFRAYGSPQS
FLASESLIDELAEKMGIDPLELRARNVYRPGDTTPTGQVPEVFCFQEMIEKLRPIYTSAL
EKAGQNSTADVKRGVGISLGIYGCGLDGADSSEIRVALNPDNTITVFSSWEDHGQGADMG
ALGTAHKAFEPMGVQPDRIRLVMNDTAITPNSGPAGGSRSQVVTGNAIKNGCEMLMAAMR
KPDGTYRTFAEMEAENLPVSYSGQWTASMCTNCDLKTSQGEPFSVYMYGMFMAEVAVETA
TGKTTVEGFTAISDVGSINNKLVVDGQMYGGIAQGIGLALSEDFEDLSKHNNLRACGLPY
AKMIPDKMDLHYIESPRENGPFGAAGVGELPLTSSHVAVINAIHNACGVRIRHLPALPEK
VLAALKK

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