Structure of PDB 7aau Chain D

Receptor sequence
>7aauD (length=378) Species: 3055 (Chlamydomonas reinhardtii) [Search protein sequence]
MSETAGKPIECKAAIAWEAKKPLEVRTVTVAPPGPGEVRVQIKATALCQT
DAYTLGGLDPEGRFPCILGHEAAGVVESVGEGVTSVKPGDHVIPCYQAYC
GECKFCKHPESNLCVSVRAFTGKGVMKSDGKPRFTVDGKPIYHFMGTSTF
SEYTVVHEQSVAKIDVNAPLDKVCLLGCGVSTGWGAVFNTAKVTAGSTVA
VFGLGAVGLAVIEAAKRAGASRIIAVDIDPTKFPTAKEFGATDCINPKDH
EKPIQQVIVEMTEWGCDYTFECIGNTAVMRAALECAHRGWGTSVIVGVAA
AGQEISTRPFQLVTGRRWMGTAFGGYKSRVQVPDLVTDYMSGATLLDKYI
THNMKFDQINEAFELLHAGECLRCVLTF
3D structure
PDB7aau Structural and functional insights into nitrosoglutathione reductase from Chlamydomonas reinhardtii.
ChainD
Resolution2.301 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) C48 T50 Y53 H70 C178
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 D C48 H70 E71 C178 C48 H70 E71 C178
BS02 ZN D C100 C103 C106 C114 C100 C103 C106 C114
BS03 NAD D T182 G205 V207 D227 I228 K232 C272 I273 V296 G297 V298 A322 F323 R373 T182 G205 V207 D227 I228 K232 C272 I273 V296 G297 V298 A322 F323 R373
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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Cellular Component
External links
PDB RCSB:7aau, PDBe:7aau, PDBj:7aau
PDBsum7aau
PubMed33316743
UniProtA0A2K3D6R4

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