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5VV7

Structure of bovine endothelial nitric oxide synthase heme domain in complex with 7-(((3-(Pyridin-3-yl)propyl)amino)methyl)quinolin-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 Residues16
Detailsbinding site for residue HEM A 501
ChainResidue
ATRP180
AGLU363
APHE475
ATYR477
AH4B502
AXH8503
AHOH620
AHOH621
AARG185
ACYS186
AVAL187
ASER228
APHE355
ASER356
ATRP358
AMET360

site_idAC2
Number of Residues11
Detailsbinding site for residue H4B A 502
ChainResidue
ASER104
AARG367
AALA448
ATRP449
AHEM501
AGOL504
AHOH620
AHOH673
BTRP447
BPHE462
BHIS463

site_idAC3
Number of Residues5
Detailsbinding site for residue XH8 A 503
ChainResidue
AVAL338
ATRP358
AGLU363
AHEM501
AGOL504

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 504
ChainResidue
AARG367
AHIS373
AH4B502
AXH8503
BTRP76
BHIS463

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 505
ChainResidue
ACYS96
ACYS101
BCYS96
BCYS101

site_idAC6
Number of Residues15
Detailsbinding site for residue HEM B 501
ChainResidue
BTRP180
BALA183
BARG185
BCYS186
BVAL187
BSER228
BPHE355
BSER356
BTRP358
BGLU363
BTYR477
BH4B502
BXH8503
BHOH604
BHOH675

site_idAC7
Number of Residues13
Detailsbinding site for residue H4B B 502
ChainResidue
ATRP447
APHE462
AHIS463
AGLN464
AGLU465
BSER104
BARG367
BALA448
BTRP449
BHEM501
BGOL504
BHOH638
BHOH675

site_idAC8
Number of Residues6
Detailsbinding site for residue XH8 B 503
ChainResidue
BVAL338
BTRP358
BGLU363
BTYR477
BHEM501
BGOL504

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL B 504
ChainResidue
BVAL106
BARG367
BHIS373
BH4B502
BXH8503

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 2024-07-24

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