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Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.

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 950
ChainResidue
ACYS326
ACYS326
ACYS331
ACYS331

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 900
ChainResidue
ATRP409
AARG414
ACYS415
AVAL416
ASER457
APHE584
ASER585
ATRP587
AGLU592
ATRP678
ATYR706
AH4B901
A3AR902
AHOH8
AHOH23
AHOH82
AHOH85
AHOH200

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE H4B A 901
ChainResidue
AHOH5
AHOH12
AHOH22
AHOH23
AHOH114
ASER334
AARG596
ATRP676
AVAL677
ATRP678
APHE691
AHIS692
AGLN693
AGLU694
AHEM900

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 3AR A 902
ChainResidue
AHOH48
AHOH82
AHOH126
AGLN478
ATYR562
APRO565
AVAL567
APHE584
ASER585
AGLY586
ATRP587
ATYR588
AGLU592
AASP597
AHEM900

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

218853

PDB entries from 2024-04-24

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