Structure of PDB 4xyb Chain A

Receptor sequence
>4xybA (length=384) Species: 682795 (Granulicella mallensis MP5ACTX8) [Search protein sequence]
AKVLCVLYDDPTSGYPPLYARNAIPKIERYPDGQTVPNPKHIDFVPGELL
GCVSGELGLRSYLEDLGHTFIVTSDKEGPNSVFEKELPDADIVISQPFWP
AYLTAERIAKAKKLKLALTAGIGSDHVDLNAAIKAGITVAEETFSNGICV
AEHAVMMILALVRNYLPSHKIAEEGGWNIADCVSRSYDLEGMHVGTVAAG
RIGLAVLRRLKPFDVKLHYTARHRSPRAIEDELGLTYHATAEEMAEVCDV
ISIHAPLYPATEHLFNAKVLNKMRHGSYLVNTARAEICDRDDIVRALESG
QLAGYAGDVWFPQPAPANHPWRNMPHNGMTPHMSGSSLSGQARYAAGTRE
ILECWFENRPIRDEYLIVSNGKLAGTGAKSYGVG
3D structure
PDB4xyb Structural basis for double cofactor specificity in a new formate dehydrogenase from the acidobacterium Granulicella mallensis MP5ACTX8.
ChainA
Resolution1.38 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N147 R285 D309 Q314 H333
Catalytic site (residue number reindexed from 1) N146 R284 D308 Q313 H332
Enzyme Commision number 1.17.1.9: formate dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NDP A I123 N147 V151 A199 G201 R202 I203 R223 H224 P257 Y259 T262 T283 A284 R285 D309 H333 S335 G336 S381 I122 N146 V150 A198 G200 R201 I202 R222 H223 P256 Y258 T261 T282 A283 R284 D308 H332 S334 G335 S380
BS02 AZI A P98 F99 I123 R285 H333 P97 F98 I122 R284 H332
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008863 formate dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding
Biological Process
GO:0042183 formate catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:4xyb, PDBe:4xyb, PDBj:4xyb
PDBsum4xyb
PubMed26104866
UniProtG8NVB5

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