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3RQP

Structure of the endothelial nitric oxide synthase heme domain in complex with 6-{[(3R,4R)-4-(2-{[(2R/2S)-1-(3-fluorophenyl)propan-2-yl]amino}ethoxy)pyrrolidin-3-yl]methyl}-4-methylpyridin-2-amine

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 500
ChainResidue
ATRP180
AH4B600
AX2E805
AARG185
ACYS186
ASER228
APHE355
ASER356
ATRP358
AGLU363
APHE475

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE H4B A 600
ChainResidue
ASER104
AARG367
AALA448
ATRP449
AHEM500
AX2E805
AGOL880
AHOH1094
BTRP447
BPHE462
BHIS463
BGLN464
BHOH1125

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE X2E A 805
ChainResidue
AVAL106
AARG185
APRO336
APHE355
ASER356
AGLY357
ATRP358
AGLU363
ATRP449
ATYR477
AHEM500
AH4B600
AGOL880

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 860
ChainResidue
ATRP358
AVAL420
ASER428
AHOH1079

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 880
ChainResidue
AARG367
AHIS373
AH4B600
AX2E805
BHOH1125

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CAD A 950
ChainResidue
ATRP324
ACYS384
ALYS438
AALA439
AARG440
AGLY441

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 900
ChainResidue
ACYS96
ACYS101
BCYS96
BCYS101

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BTRP180
BARG185
BCYS186
BSER228
BPHE355
BSER356
BTRP358
BGLU363
BPHE475
BH4B600
BX2E805
BHOH1047

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE H4B B 600
ChainResidue
ATRP447
APHE462
BSER104
BARG367
BALA448
BTRP449
BHEM500
BX2E805
BGOL880
BHOH1061
BHOH1075
BHOH1123

site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE X2E B 805
ChainResidue
BVAL106
BLEU107
BARG185
BGLN249
BPRO336
BGLY357
BTRP358
BGLU363
BTRP449
BTYR477
BHEM500
BH4B600
BGOL880

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 860
ChainResidue
BILE190
BTRP358
BVAL420
BSER428

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 880
ChainResidue
BHIS373
BH4B600
BX2E805
BHOH1123
BVAL106
BARG367

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CAD B 950
ChainResidue
BTYR83
BTRP324
BCYS384

Functional Information from PROSITE/UniProt
site_idPS60001
Number of Residues8
DetailsNOS Nitric oxide synthase (NOS) signature. RCVGRIqW
ChainResidueDetails
AARG185-TRP192

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P35228
ChainResidueDetails
ACYS96
ACYS101
BCYS96
BCYS101

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P29474
ChainResidueDetails
ASER104
ATYR477
BSER104
BGLN249
BTRP358
BTYR359
BGLU363
BASN368
BALA448
BTRP449
BPHE462
AGLN249
BTYR477
ATRP358
ATYR359
AGLU363
AASN368
AALA448
ATRP449
APHE462

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P29474
ChainResidueDetails
ACYS186
BCYS186

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK5 => ECO:0000250|UniProtKB:P29474
ChainResidueDetails
ASER116
BSER116

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PDB entries from 2024-04-24

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