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1M7V

STRUCTURE OF A NITRIC OXIDE SYNTHASE HEME PROTEIN FROM BACILLUS SUBTILIS WITH TETRAHYDROFOLATE AND ARGININE BOUND

Functional Information from GO Data
ChainGOidnamespacecontents
A0004517molecular_functionnitric-oxide synthase activity
A0006809biological_processnitric oxide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ARG A 2000
ChainResidue
AGLN125
AHOH2007
AHOH2045
AARG128
ATYR209
AILE214
ATRP234
ATYR235
AGLU239
AASN244
AHEM901

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 901
ChainResidue
ATRP56
ASER59
ACYS62
APHE231
AASN232
AGLY233
ATRP234
AGLU239
ATRP325
ATYR351
ATYR353
ATHG1999
AARG2000
AHOH2051
AHOH2082
AHOH2148
AHOH2220

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE THG A 1999
ChainResidue
AARG243
AASP322
ATRP323
ATHR324
ATRP325
APHE338
AARG340
ASER341
ATYR342
AASN344
AHEM901
AHOH2301
AHOH2325

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 site: {"description":"axial binding residue"}
ChainResidueDetails

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

246704

PDB entries from 2025-12-24

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