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5G65

Structure of Bacillus subtilis Nitric Oxide Synthase in complex with quinolin-2-amine

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 1364
ChainResidue
ATRP60
ATRP329
ATYR355
ATYR357
A2AQ1366
APEG1368
AHOH2156
AHOH2170
AHOH2172
AHOH2173
ASER63
AARG65
ACYS66
APHE235
AASN236
AGLY237
ATRP238
AGLU243

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1365
ChainResidue
AGLN129
AARG132
ATYR239
AASN248

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 2AQ A 1366
ChainResidue
AILE218
APHE235
ATRP238
ATYR239
AGLU243
AHEM1364

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1367
ChainResidue
AHIS128
AASP220
AMET221
ALYS360
AHOH2168
AHOH2169

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 1368
ChainResidue
AARG247
ATRP327
APHE342
AARG344
AHEM1364

Functional Information from PROSITE/UniProt
site_idPS60001
Number of Residues8
DetailsNOS Nitric oxide synthase (NOS) signature. RCIGRLfW
ChainResidueDetails
AARG65-TRP72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS66

221051

PDB entries from 2024-06-12

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