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5UX9

The crystal structure of chloramphenicol acetyltransferase from Vibrio fischeri ES114

Functional Information from GO Data
ChainGOidnamespacecontents
A0008811molecular_functionchloramphenicol O-acetyltransferase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0008811molecular_functionchloramphenicol O-acetyltransferase activity
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
C0008811molecular_functionchloramphenicol O-acetyltransferase activity
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
D0008811molecular_functionchloramphenicol O-acetyltransferase activity
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0046677biological_processresponse to antibiotic
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MES A 301
ChainResidue
APHE98
APRO99
ASER101
APHE105
BGLY10
BTYR27
BTYR29

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 302
ChainResidue
AHOH402
AHOH418
AHIS204
AGLU207

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 303
ChainResidue
AASP26
ATYR27
ALYS72
ATRP186
ATRP188

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 305
ChainResidue
AHIS90
BTYR29

site_idAC5
Number of Residues6
Detailsbinding site for residue MES B 301
ChainResidue
BPHE98
BPRO99
BSER101
BPHE105
CGLY10
CTYR29

site_idAC6
Number of Residues3
Detailsbinding site for residue MG B 302
ChainResidue
BHIS204
BGLU207
BHOH411

site_idAC7
Number of Residues2
Detailsbinding site for residue ACT B 303
ChainResidue
BPHE62
CLEU8

site_idAC8
Number of Residues2
Detailsbinding site for residue CL B 304
ChainResidue
BTRP186
BTRP188

site_idAC9
Number of Residues1
Detailsbinding site for residue CL B 305
ChainResidue
BASP111

site_idAD1
Number of Residues2
Detailsbinding site for residue CL B 306
ChainResidue
BHIS90
CTYR29

site_idAD2
Number of Residues6
Detailsbinding site for residue MES C 301
ChainResidue
ALEU8
AGLY10
CPHE98
CPRO99
CSER101
CPHE105

site_idAD3
Number of Residues4
Detailsbinding site for residue MES C 302
ChainResidue
CPHE62
CALA85
CASP111
CPHE113

site_idAD4
Number of Residues6
Detailsbinding site for residue MG C 303
ChainResidue
CHIS204
CGLU207
CHOH406
CHOH416
CHOH419
CHOH422

site_idAD5
Number of Residues4
Detailsbinding site for residue ACT C 304
ChainResidue
CASP26
CTYR27
CTRP186
CTRP188

site_idAD6
Number of Residues3
Detailsbinding site for residue ACT C 305
ChainResidue
CGLU64
CLYS67
DASN195

site_idAD7
Number of Residues2
Detailsbinding site for residue CL C 306
ChainResidue
ATYR29
CHIS90

site_idAD8
Number of Residues8
Detailsbinding site for residue MES D 301
ChainResidue
DGLY10
DTYR27
DTYR29
DPHE98
DPRO99
DPHE100
DSER101
DPHE105

site_idAD9
Number of Residues4
Detailsbinding site for residue MES D 302
ChainResidue
DGLN88
DASP111
DPHE113
DACT304

site_idAE1
Number of Residues3
Detailsbinding site for residue MG D 303
ChainResidue
DHIS204
DGLU207
DHOH427

site_idAE2
Number of Residues4
Detailsbinding site for residue ACT D 304
ChainResidue
DLEU48
DPHE62
DPHE113
DMES302

site_idAE3
Number of Residues2
Detailsbinding site for residue CL D 305
ChainResidue
DTYR29
DHIS90

site_idAE4
Number of Residues4
Detailsbinding site for residue FMT D 306
ChainResidue
DASP26
DLYS72
DTRP186
DTRP188

Functional Information from PROSITE/UniProt
site_idPS00101
Number of Residues29
DetailsHEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. IGseAmImpgVhIGdgAiIGarAvItknV
ChainResidueDetails
AILE127-VAL155

221051

PDB entries from 2024-06-12

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