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5VVA

Structure of bovine endothelial nitric oxide synthase heme domain in complex with 4-(2-(((2-Amino-4-methylquinolin-7-yl)methyl)amino)ethyl)-2-methylbenzonitrile

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 Residues15
Detailsbinding site for residue HEM A 501
ChainResidue
ATRP180
ATRP449
APHE475
ATYR477
AH4B502
A9OJ503
AHOH601
AARG185
ACYS186
ASER228
APHE355
ASER356
ATRP358
AMET360
AGLU363

site_idAC2
Number of Residues10
Detailsbinding site for residue H4B A 502
ChainResidue
ASER104
AVAL106
AARG367
AALA448
ATRP449
AHEM501
AGOL504
AHOH601
BPHE462
BGLN464

site_idAC3
Number of Residues8
Detailsbinding site for residue 9OJ A 503
ChainResidue
ALEU107
APRO336
AVAL338
ATRP358
ATYR359
AGLU363
AHEM501
BTRP76

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 504
ChainResidue
AARG367
AHIS373
AH4B502
BTRP76
BHIS463

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

site_idAC6
Number of Residues14
Detailsbinding site for residue HEM B 501
ChainResidue
BTRP180
BALA183
BCYS186
BSER228
BMET341
BPHE355
BSER356
BTRP358
BMET360
BGLU363
BPHE475
BTYR477
BH4B502
B9OJ503

site_idAC7
Number of Residues8
Detailsbinding site for residue H4B B 502
ChainResidue
ATRP447
APHE462
BSER104
BARG367
BALA448
BTRP449
BHEM501
BGOL504

site_idAC8
Number of Residues9
Detailsbinding site for residue 9OJ B 503
ChainResidue
ATRP76
BLEU107
BVAL338
BTRP358
BGLU363
BTRP449
BTYR477
BHEM501
BGOL504

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL B 504
ChainResidue
BVAL106
BARG367
BHIS373
BTRP449
BH4B502
B9OJ503

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 2024-05-01

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