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5KOW

Structure of rifampicin monooxygenase

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 Residues29
Detailsbinding site for residue FAD A 501
ChainResidue
AGLY8
AGLN98
ACYS120
AGLU121
AVAL122
ACYS150
AASP151
AGLY152
ATHR156
ALEU176
AGLY275
AGLY10
AASP276
APRO283
AGLN287
AGLY288
ALEU289
AASN290
AHOH608
AHOH612
AHOH619
AHOH641
APRO11
ATHR12
ALEU30
AGLU31
ALYS32
AARG41
ASER42

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 502
ChainResidue
AGLY162
AGLY407
AARG409
AHOH666

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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