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5KOX

Structure of rifampicin monooxygenase complexed with rifampicin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004497molecular_functionmonooxygenase activity
A0016709molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
A0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues36
Detailsbinding site for residue FAD A 501
ChainResidue
AGLY8
AARG43
AGLY44
AGLN98
ACYS120
AGLU121
AVAL122
ACYS150
AASP151
AGLY152
ATHR156
AGLY10
ALEU176
AGLY275
AASP276
APRO283
AGLY286
AGLN287
AGLY288
ALEU289
AASN290
ARFP502
APRO11
AHOH609
AHOH610
AHOH629
AHOH643
AHOH662
AHOH679
AHOH735
ATHR12
ALEU30
AGLU31
ALYS32
AARG41
ASER42

site_idAC2
Number of Residues16
Detailsbinding site for residue RFP A 502
ChainResidue
AARG43
AGLY44
APHE74
ALEU200
AGLY203
AVAL205
AILE215
APHE256
APRO283
ATHR284
AGLY285
AGLY286
AFAD501
AHOH612
AHOH640
AHOH706

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:27557658, ECO:0000269|PubMed:29578336, ECO:0007744|PDB:5KOW, ECO:0007744|PDB:5KOX, ECO:0007744|PDB:6C7S
ChainResidueDetails
ATHR12
AASN290
AGLU31
ALYS32
AARG41
AGLN98
AVAL122
ATHR156
AASP276
ALEU289

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27557658, ECO:0000269|PubMed:29578336, ECO:0007744|PDB:5KOX, ECO:0007744|PDB:6C7S
ChainResidueDetails
AARG43
AGLY285

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:29578336, ECO:0007744|PDB:6C7S
ChainResidueDetails
AARG196

223166

PDB entries from 2024-07-31

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