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1M7Z

Structure of Nitric Oxide Synthase Heme Protein from Bacillus Subtilis with N-Hydroxy-Arginine and Tetrahydrofolate Bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004517molecular_functionnitric-oxide synthase activity
A0005575cellular_componentcellular_component
A0006809biological_processnitric oxide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 901
ChainResidue
ATRP56
ATRP325
ATYR351
ATYR353
AHAR909
AHOH957
AHOH975
AHOH991
AHOH1029
ATHG1999
ASER59
AARG61
ACYS62
APHE231
AASN232
AGLY233
ATRP234
AGLU239

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HAR A 909
ChainResidue
AGLN125
AARG128
ATYR209
AILE214
AGLY233
ATRP234
ATYR235
AGLU239
AASN244
AHEM901
AHOH945
AHOH1015
AHOH1198

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE THG A 1999
ChainResidue
AARG243
ATRP323
ATHR324
ATRP325
APHE338
AARG340
ATYR342
AHEM901
AHOH1149
AHOH1182
AHOH1187
AHOH1194

Functional Information from PROSITE/UniProt
site_idPS60001
Number of Residues8
DetailsNOS Nitric oxide synthase (NOS) signature. RCIGRLfW
ChainResidueDetails
AARG61-TRP68

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ALEU89

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 3nos
ChainResidueDetails
ATRP234
ACYS62
AARG65
AGLU239

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PDB entries from 2024-07-17

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