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4D1O

Structure of human endothelial nitric oxide synthase heme domain with L-Arg bound

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 Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
ATRP178
ATRP447
APHE473
ATYR475
AARG700
AACT860
AH4B1481
AHOH2365
AHOH2366
AHOH2368
AHOH2369
AARG183
AHOH2370
ACYS184
ASER226
APHE353
ASER354
ATRP356
AMET358
AGLU361

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ARG A 700
ChainResidue
AGLN247
ATYR331
ATRP356
ATYR357
AGLU361
AASN366
AHEM500
AHOH2278

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 860
ChainResidue
AGLY186
ATRP356
AVAL418
ASER426
AHEM500
AHOH2128

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BTB A 870
ChainResidue
AVAL381
ACYS382
AASP384
AGD1482
AHOH2297
AHOH2298
AHOH2372
AHOH2373
AHOH2374

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BTB A 871
ChainResidue
AGLU377
AHOH2375

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 880
ChainResidue
AARG365
AHIS371
AH4B1481
AHOH2281
AHOH2282
AHOH2376

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 881
ChainResidue
AGLU167
AHOH2377
AHOH2378

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 900
ChainResidue
ACYS94
ACYS99
BCYS94
BCYS99

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE H4B A 1481
ChainResidue
ASER102
AARG365
AALA446
ATRP447
AHEM500
AGOL880
AHOH2056
AHOH2281
AHOH2339
AHOH2370
BTRP445
BPHE460
BHIS461
BGLU463

site_idBC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BTRP178
BARG183
BCYS184
BSER226
BPHE353
BSER354
BTRP356
BMET358
BGLU361
BTRP447
BPHE473
BTYR475
BARG700
BH4B1481
BHOH2373
BHOH2374
BHOH2380
BHOH2381
BHOH2382

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ARG B 700
ChainResidue
BHOH2233
BHOH2304
BGLN247
BARG250
BTYR331
BTRP356
BTYR357
BGLU361
BASN366
BHEM500

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 860
ChainResidue
BTRP356
BSER426
BHOH2140
BHOH2383

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BTB B 870
ChainResidue
BTHR319
BGLU321
BGD1482
BHOH2284
BHOH2285
BHOH2384
BHOH2385
BHOH2386

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BTB B 871
ChainResidue
BGLU298

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 880
ChainResidue
ATRP74
AHOH2350
BVAL104
BARG365
BHIS371
BH4B1481
BHOH2205

site_idBC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE H4B B 1481
ChainResidue
ATRP445
APHE460
AHIS461
AHOH2350
BSER102
BARG365
BALA446
BTRP447
BHEM500
BGOL880
BHOH2047
BHOH2361
BHOH2382

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GD A 1482
ChainResidue
ABTB870
AHOH2298
AHOH2299
AHOH2372
AHOH2373
AHOH2374
AHOH2379

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GD B 1482
ChainResidue
BTHR319
BGLU321
BBTB870
BHOH2284
BHOH2285

Functional Information from PROSITE/UniProt
site_idPS60001
Number of Residues8
DetailsNOS Nitric oxide synthase (NOS) signature. RCVGRIqW
ChainResidueDetails
AARG183-TRP190

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:18849972, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:1M9J, ECO:0007744|PDB:1M9K, ECO:0007744|PDB:1M9M, ECO:0007744|PDB:1M9Q, ECO:0007744|PDB:1M9R, ECO:0007744|PDB:3EAH, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P
ChainResidueDetails
ACYS94
ACYS99
BCYS94
BCYS99

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O
ChainResidueDetails
ASER102
ATYR475
BSER102
BGLN247
BTRP356
BTYR357
BGLU361
BASN366
BALA446
BTRP447
BPHE460
AGLN247
BTYR475
ATRP356
ATYR357
AGLU361
AASN366
AALA446
ATRP447
APHE460

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O
ChainResidueDetails
ACYS184
BCYS184

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P
ChainResidueDetails
AARG365
BARG365

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:20213743
ChainResidueDetails
ASER114
BSER114

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 935
ChainResidueDetails
ACYS184metal ligand
AARG187steric role
ATRP356electrostatic stabiliser
AGLU361electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 935
ChainResidueDetails
BCYS184metal ligand
BARG187steric role
BTRP356electrostatic stabiliser
BGLU361electrostatic stabiliser

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PDB entries from 2024-05-08

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