Structure of PDB 7aas Chain D

Receptor sequence
>7aasD (length=377) Species: 3055 (Chlamydomonas reinhardtii) [Search protein sequence]
SETAGKPIECKAAIAWEAKKPLEVRTVTVAPPGPGEVRVQIKATALCQTD
AYTLGGLDPEGRFPCILGHEAAGVVESVGEGVTSVKPGDHVIPCYQAYCG
ECKFCKHPESNLCVSVRAFTGKGVMKSDGKPRFTVDGKPIYHFMGTSTFS
EYTVVHEQSVAKIDVNAPLDKVCLLGCGVSTGWGAVFNTAKVTAGSTVAV
FGLGAVGLAVIEAAKRAGASRIIAVDIDPTKFPTAKEFGATDCINPKDHE
KPIQQVIVEMTEWGCDYTFECIGNTAVMRAALECAHRGWGTSVIVGVAAA
GQEISTRPFQLVTGRRWMGTAFGGYKSRVQVPDLVTDYMSGATLLDKYIT
HNMKFDQINEAFELLHAGECLRCVLTF
3D structure
PDB7aas Structural and functional insights into nitrosoglutathione reductase from Chlamydomonas reinhardtii.
ChainD
Resolution1.8 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 D C48 H70 E71 C178 C47 H69 E70 C177
BS02 ZN D C100 C103 C106 C114 C99 C102 C105 C113
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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Cellular Component
External links
PDB RCSB:7aas, PDBe:7aas, PDBj:7aas
PDBsum7aas
PubMed33316743
UniProtA0A2K3D6R4

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