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3N5R

Structure of endothelial nitric oxide synthase heme domain complexed with 4-(3-(2-(6-amino-4-methylpyridin-2-yl)ethyl)phenethyl)-6-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 Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
ATRP180
APHE475
ATYR477
AH4B600
AXFH800
AHOH1037
AALA183
AARG185
ACYS186
APHE355
ASER356
ATRP358
AGLU363
ATRP449

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 850
ChainResidue
AARG252
AASN368
AARG374
AHOH1048

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 860
ChainResidue
ATRP358
AVAL420
ASER428

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 880
ChainResidue
AARG367
AHIS373
AH4B600

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CAD A 950
ChainResidue
ATRP324
ACYS384
AGLN437
ALYS438
AALA439
AGLY441

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE H4B A 600
ChainResidue
ASER104
AVAL106
AARG367
AALA448
ATRP449
AHEM500
AGOL880
AHOH1037
BTRP447
BPHE462

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE XFH A 800
ChainResidue
APRO336
AVAL338
AASN340
APHE355
AGLY357
ATRP358
ATYR359
AGLU363
ATYR477
AGLN478
AHEM500

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 900
ChainResidue
ACYS96
ACYS101
BCYS96
BCYS101

site_idAC9
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BTRP180
BALA183
BARG185
BCYS186
BSER228
BPHE355
BSER356
BGLY357
BTRP358
BMET360
BGLU363
BPHE475
BTYR477
BH4B600
BXFH800
BHOH1106

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 860
ChainResidue
BILE190
BTRP358
BVAL420
BSER428

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 880
ChainResidue
ATRP76
BVAL106
BARG367
BHIS373
BH4B600

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CAD B 950
ChainResidue
BTYR83
BTRP324
BCYS384

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE H4B B 600
ChainResidue
ATRP447
APHE462
BSER104
BARG367
BALA448
BTRP449
BHEM500
BGOL880

site_idBC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE XFH B 800
ChainResidue
BGLU363
BTYR477
BHEM500
BGLN249
BPRO336
BVAL338
BASN340
BGLY357
BTRP358
BTYR359
BMET360

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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