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4K5K

Structure of bovine endothelial nitric oxide synthase heme domain in complex with ((2S, 3S)-1,3-bis((6-(2,5-dimethyl-1H-pyrrol-1-yl)-4-methylpyridin-2-yl)methoxy)-2-aminobutane

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
APHE475
ATYR477
AH4B502
AQ13503
AHOH614
AHOH635
AHOH729
AARG185
ACYS186
ASER228
APHE355
ASER356
ATRP358
AGLU363
ATRP449

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE H4B A 502
ChainResidue
ASER104
AVAL106
AARG367
AALA448
ATRP449
AHEM501
AGOL506
AHOH614
AHOH629
AHOH738
BTRP447
BPHE462
BHIS463
BGLN464
BGLU465
BHOH606

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE Q13 A 503
ChainResidue
AVAL106
ALEU107
AVAL338
APHE355
ATRP358
ATYR359
AGLU363
ATYR477
AHEM501
AACT505
AHOH728

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 504
ChainResidue
AGLY188
ATRP358
ASER428
AHOH703

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 505
ChainResidue
AGLN249
AARG252
AASN368
AARG374
AQ13503
AHOH725

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 506
ChainResidue
AVAL106
AARG367
AHIS373
ATRP449
AH4B502
BHOH606

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 507
ChainResidue
ACYS96
ACYS101
BCYS96
BCYS101

site_idAC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 501
ChainResidue
BTRP180
BARG185
BCYS186
BSER228
BPHE355
BSER356
BTRP358
BGLU363
BTRP449
BTYR477
BH4B502
BQ13503
BHOH608
BHOH642
BHOH680

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE H4B B 502
ChainResidue
ATRP447
APHE462
AHIS463
AGLU465
AHOH610
BSER104
BARG367
BALA448
BTRP449
BHEM501
BGOL506
BHOH608
BHOH658
BHOH659

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE Q13 B 503
ChainResidue
BGLU363
BTYR477
BHEM501
BACT505
BHOH730
BVAL106
BLEU107
BPRO336
BVAL338
BPHE355
BTRP358
BTYR359

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 504
ChainResidue
BTRP358
BSER428
BHOH759
BHOH760

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 505
ChainResidue
BGLN249
BARG252
BASN368
BARG374
BQ13503
BHOH615

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 506
ChainResidue
AHOH610
BVAL106
BARG367
BHIS373
BTRP449
BH4B502

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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