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1NOC

MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114) COMPLEXED WITH TYPE I E. COLI CHLORAMPHENICOL ACETYL TRANSFERASE AND IMIDAZOLE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004517molecular_functionnitric-oxide synthase activity
A0006809biological_processnitric oxide biosynthetic process
A0020037molecular_functionheme binding
B0008811molecular_functionchloramphenicol O-acetyltransferase activity
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 901
ChainResidue
ATRP188
ATRP366
ATYR483
ATYR485
AIMD902
AIMD903
AHOH1029
AARG193
ACYS194
AILE195
AGLN199
ASER236
APHE363
AASN364
AGLY365

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IMD A 902
ChainResidue
APRO344
AHEM901
AIMD903

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD A 903
ChainResidue
ATRP366
ATYR367
AGLU371
AHEM901
AIMD902

Functional Information from PROSITE/UniProt
site_idPS00100
Number of Residues11
DetailsCAT Chloramphenicol acetyltransferase active site. QVHHAvcDGFH
ChainResidueDetails
BGLN190-HIS200

site_idPS60001
Number of Residues8
DetailsNOS Nitric oxide synthase (NOS) signature. RCIGRIqW
ChainResidueDetails
AARG193-TRP200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
BHIS193

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P29474
ChainResidueDetails
AGLN257
ATRP366
ATYR367
AGLU371

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1JWK, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:3NOD
ChainResidueDetails
AARG375

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N
ChainResidueDetails
AILE456

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD
ChainResidueDetails
ATRP457

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1JWK, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD
ChainResidueDetails
APHE470

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD
ChainResidueDetails
ATYR485

218853

PDB entries from 2024-04-24

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