Structure of PDB 7av7 Chain B

Receptor sequence
>7av7B (length=377) Species: 3055 (Chlamydomonas reinhardtii) [Search protein sequence]
SETAGKPIECKAAIAWEAKKPLEVRTVTVAPPGPGEVRVQIKATALCQTD
AYTLGGLDPEGRFPCILGHEAAGVVESVGEGVTSVKPGDHVIPCYQAYCG
ECKFCKHPESNLCVSVRAFTGKGVMKSDGKPRFTVDGKPIYHFMGTSTFS
EYTVVHEQSVAKIDVNAPLDKVCLLGCGVSTGWGAVFNTAKVTAGSTVAV
FGLGAVGLAVIEAAKRAGASRIIAVDIDPTKFPTAKEFGATDCINPKDHE
KPIQQVIVEMTEWGCDYTFECIGNTAVMRAALECAHRGWGTSVIVGVAAA
GQEISTRPFQLVTGRRWMGTAFGGYKSRVQVPDLVTDYMSGATLLDKYIT
HNMKFDQINEAFELLHAGECLRCVLTF
3D structure
PDB7av7 Structural and functional insights into nitrosoglutathione reductase from Chlamydomonas reinhardtii.
ChainB
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C48 T50 Y53 H70 C178
Catalytic site (residue number reindexed from 1) C47 T49 Y52 H69 C177
Enzyme Commision number 1.1.1.284: S-(hydroxymethyl)glutathione 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 ZN B C48 H70 E71 C178 C47 H69 E70 C177
BS02 ZN B C100 C103 C106 C114 C99 C102 C105 C113
BS03 NAD B Q49 Y96 C178 T182 G205 V207 D227 I228 K232 C272 I273 V296 G297 V298 A322 F323 Q48 Y95 C177 T181 G204 V206 D226 I227 K231 C271 I272 V295 G296 V297 A321 F322
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004022 alcohol dehydrogenase (NAD+) activity
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051903 S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
GO:0106321 S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
GO:0106322 S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
Biological Process
GO:0044281 small molecule metabolic process
GO:0046294 formaldehyde catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7av7, PDBe:7av7, PDBj:7av7
PDBsum7av7
PubMed33316743
UniProtA0A2K3D6R4

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