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3JX4

Structure of rat neuronal nitric oxide synthase D597N/M336V mutant heme domain in complex with N1-{(3'R,4'S)-4'-[(6"-amino-4"-methylpyridin-2"-yl)methyl]pyrrolidin-3'-yl}-N2-(3'-fluorophenethyl)ethane-1,2-diamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004517molecular_functionnitric-oxide synthase activity
A0006809biological_processnitric oxide biosynthetic process
B0004517molecular_functionnitric-oxide synthase activity
B0006809biological_processnitric oxide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM A 750
ChainResidue
ATRP409
AJ11800
AACT860
AALA412
AARG414
ACYS415
APHE584
ASER585
ATRP587
ATYR706
AH4B760

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE H4B A 760
ChainResidue
ASER334
AVAL336
AARG596
AVAL677
ATRP678
AHEM750
AHOH1011
BTRP676
BPHE691
BHIS692
BGLN693
BGLU694

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE J11 A 800
ChainResidue
AVAL567
APHE584
ATRP587
AGLU592
AHEM750
AHOH1000
BTRP306

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 860
ChainResidue
AILE419
ATRP587
AHEM750

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 900
ChainResidue
ACYS326
ACYS331
BCYS326
BCYS331

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 750
ChainResidue
BTRP409
BALA412
BARG414
BCYS415
BPHE584
BSER585
BGLY586
BTRP587
BGLU592
BTRP678
BPHE704
BTYR706
BH4B760
BJ11800
BHOH1042

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE H4B B 760
ChainResidue
ATRP676
APHE691
AHIS692
AGLN693
AGLU694
BSER334
BARG596
BVAL677
BTRP678
BHEM750
BHOH1004

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE J11 B 800
ChainResidue
BVAL336
BVAL567
BGLY586
BTRP587
BTYR588
BGLU592
BTYR706
BHEM750
BHOH1000
BHOH1009

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 860
ChainResidue
BGLN420
BTRP587
BSER657

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 Residues18
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P29475
ChainResidueDetails
ATRP587
ATYR588
AGLU592
AVAL677
ATRP678
APHE691
ATYR706
BSER334
BGLN478
BTRP587
BTYR588
BGLU592
BVAL677
BTRP678
BPHE691
BTYR706
ASER334
AGLN478

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P29475
ChainResidueDetails
ACYS415
BCYS415

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PDB entries from 2024-04-17

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