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4D1P

Structure of human endothelial nitric oxide synthase heme domain IN COMPLEX WITH 6-((((3S, 5R)-5-(((6-AMINO-4-METHYLPYRIDIN-2-YL)METHOXY) METHYL)PYRROLIDIN-3-YL)OXY) METHYL)-4-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 Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
ATRP178
ATYR475
AH4B600
AQ16800
AHOH2370
AHOH2372
AHOH2373
ACYS184
ASER226
APHE353
ASER354
ATRP356
AMET358
AGLU361
APHE473

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE H4B A 600
ChainResidue
ASER102
AARG365
AALA446
ATRP447
AHEM500
AHOH2049
AHOH2282
AHOH2349
AHOH2372
AHOH2374
BTRP445
BPHE460
BHIS461

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE Q16 A 800
ChainResidue
APHE105
AVAL336
APHE353
ATRP356
AGLU361
AHEM500
AHOH2283
AHOH2374
BTRP74

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 861
ChainResidue
AARG250
AASN366
AARG372
AHOH2204

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BTB A 870
ChainResidue
ACYS382
AASP384
AGD1490
AHOH2298
AHOH2299
AHOH2300
AHOH2375
AHOH2376
AHOH2377

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BTB A 871
ChainResidue
AGLU377
AHOH2295

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 880
ChainResidue
AGLU167
AHOH2105
AHOH2378
AHOH2379

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

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 860
ChainResidue
ATRP356
AVAL418
ASER426
AHOH2133
AHOH2327

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GD A 1490
ChainResidue
ABTB870
AHOH2299
AHOH2300
AHOH2375
AHOH2376
AHOH2377
AHOH2381

site_idBC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BTRP178
BCYS184
BSER226
BPHE353
BSER354
BTRP356
BGLU361
BTRP447
BPHE473
BTYR475
BH4B600
BQ16800
BHOH2285
BHOH2357
BHOH2358
BHOH2363
BHOH2364

site_idBC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE H4B B 600
ChainResidue
BHOH2346
BHOH2363
BHOH2365
ATRP445
APHE460
AHIS461
AHOH2358
BSER102
BARG365
BALA446
BTRP447
BHEM500
BHOH2042

site_idBC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE Q16 B 800
ChainResidue
BPHE105
BVAL336
BPHE353
BTRP356
BGLU361
BHEM500
BHOH2202
BHOH2285
BHOH2358
BHOH2365

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 860
ChainResidue
BGLY186
BTRP356
BSER426
BHOH2131
BHOH2328

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 861
ChainResidue
BARG250
BASN366
BARG372
BHOH2207
BHOH2367

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BTB B 870
ChainResidue
BTHR319
BGLU321
BGD1490
BHOH2269
BHOH2270
BHOH2368
BHOH2369
BHOH2370
BHOH2371

site_idBC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BTB B 871
ChainResidue
BGLU298

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GD B 1490
ChainResidue
BTHR319
BGLU321
BBTB870
BHOH2269
BHOH2270

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 2024-07-17

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