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1ZVI

Rat Neuronal Nitric Oxide Synthase Oxygenase Domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004517molecular_functionnitric-oxide synthase activity
A0006809biological_processnitric oxide biosynthetic process
A0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 902
ChainResidue
ACYS326
ACYS326
ACYS331
ACYS331

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM A 900
ChainResidue
ASER585
ATRP587
AMET589
AGLU592
ATRP678
ATYR706
AH4B901
AHOH1019
ATRP409
AARG414
ACYS415
ASER457
APHE584

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE H4B A 901
ChainResidue
ASER334
AARG596
ATRP676
AVAL677
ATRP678
APHE691
AHIS692
AGLN693
AGLU694
AHEM900
AHOH1002
AHOH1009
AHOH1019
AHOH1071
AHOH1119

Functional Information from PROSITE/UniProt
site_idPS60001
Number of Residues8
DetailsNOS Nitric oxide synthase (NOS) signature. RCVGRIqW
ChainResidueDetails
AARG414-TRP421

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P29475
ChainResidueDetails
ASER334
AGLN478
ATRP587
ATYR588
AGLU592
AVAL677
ATRP678
APHE691
ATYR706

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P29475
ChainResidueDetails
ACYS415

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 3nos
ChainResidueDetails
ACYS415
ATRP587
AGLU592
AARG418

222036

PDB entries from 2024-07-03

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