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1M9R

human endothelial nitric oxide synthase with 3-Bromo-7-Nitroindazole bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004517molecular_functionnitric-oxide synthase activity
A0006809biological_processnitric oxide biosynthetic process
A0020037molecular_functionheme binding
B0004517molecular_functionnitric-oxide synthase activity
B0006809biological_processnitric oxide biosynthetic process
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 904
ChainResidue
ACYS94
ACYS99
BCYS94
BCYS99

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HEM A 901
ChainResidue
ATRP356
AGLU361
ATYR475
AINE906
ATRP178
ACYS184
AMET339
APHE353
ASER354

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM B 901
ChainResidue
BTRP178
BARG183
BCYS184
BMET339
BPHE353
BSER354
BTRP356
BGLU361
BTYR475
BINE907

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE INE A 906
ChainResidue
APRO334
APHE353
ASER354
AGLY355
ATRP356
ATYR357
AMET358
AGLU361
AHEM901

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE INE B 907
ChainResidue
BPRO334
BPHE353
BSER354
BGLY355
BTRP356
BTYR357
BMET358
BGLU361
BHEM901

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE INE B 902
ChainResidue
ASER102
AARG365
ATRP447
BTRP74
BTRP445
BPHE460
BHIS461
BGLN462
BGLU463

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE INE A 903
ChainResidue
ATRP74
ATRP445
APHE460
AHIS461
AGLN462
AGLU463
BSER102
BARG365
BALA446
BTRP447

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
ATHR95
ALEU100
BTHR95
BLEU100

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O
ChainResidueDetails
ALEU103
AGLN476
BLEU103
BLEU248
BTYR357
BMET358
BILE362
BLEU367
BTRP447
BILE448
BHIS461
ALEU248
BGLN476
ATYR357
AMET358
AILE362
ALEU367
ATRP447
AILE448
AHIS461

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O
ChainResidueDetails
AVAL185
BVAL185

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
AASN366
BASN366

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:20213743
ChainResidueDetails
APRO115
BPRO115

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 3nos
ChainResidueDetails
ATRP356
AARG187
AGLU361
ACYS184

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 3nos
ChainResidueDetails
BTRP356
BARG187
BGLU361
BCYS184

site_idMCSA1
Number of Residues4
DetailsM-CSA 935
ChainResidueDetails
AVAL185metal ligand
AILE188steric role
ATYR357electrostatic stabiliser
AILE362electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 935
ChainResidueDetails
BVAL185metal ligand
BILE188steric role
BTYR357electrostatic stabiliser
BILE362electrostatic stabiliser

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PDB entries from 2024-07-24

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