Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6PUA

The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae

Functional Information from GO Data
ChainGOidnamespacecontents
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0046677biological_processresponse to antibiotic
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0046677biological_processresponse to antibiotic
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MPD A 301
ChainResidue
ATRP183
ASER187
AASN202
ALYS206

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 302
ChainResidue
AHIS37
AASP41

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 303
ChainResidue
AHIS113
AHIS131
AHOH518

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 304
ChainResidue
AASN2
ATYR33
BASP41

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 305
ChainResidue
AGLN76
CPHE8

site_idAC6
Number of Residues1
Detailsbinding site for residue EDO A 306
ChainResidue
APHE8

site_idAC7
Number of Residues4
Detailsbinding site for residue MPD A 307
ChainResidue
ATRP116
ASER137
AHOH448
BMET124

site_idAC8
Number of Residues3
Detailsbinding site for residue CL A 308
ChainResidue
AASN154
BASN154
CASN154

site_idAC9
Number of Residues3
Detailsbinding site for residue PO4 A 309
ChainResidue
AHIS47
ATYR90
APHE103

site_idAD1
Number of Residues3
Detailsbinding site for residue EDO B 301
ChainResidue
AHOH517
BARG79
BTRP82

site_idAD2
Number of Residues3
Detailsbinding site for residue EDO B 302
ChainResidue
BHIS113
BASN178
BHOH477

site_idAD3
Number of Residues1
Detailsbinding site for residue EDO B 303
ChainResidue
BPHE8

site_idAD4
Number of Residues2
Detailsbinding site for residue PO4 B 304
ChainResidue
BPHE8
CHIS47

site_idAD5
Number of Residues4
Detailsbinding site for residue MPD B 305
ChainResidue
BTRP116
BSER137
BHOH423
BHOH488

site_idAD6
Number of Residues3
Detailsbinding site for residue PO4 B 306
ChainResidue
APHE8
BHIS47
BTYR90

site_idAD7
Number of Residues6
Detailsbinding site for residue MPD B 307
ChainResidue
BTRP183
BGLU186
BSER187
BSER190
BASN202
BLYS206

site_idAD8
Number of Residues4
Detailsbinding site for residue PO4 C 301
ChainResidue
CHIS113
CASN178
CHOH428
CHOH461

site_idAD9
Number of Residues1
Detailsbinding site for residue PO4 C 302
ChainResidue
CSER187

site_idAE1
Number of Residues1
Detailsbinding site for residue EDO C 303
ChainResidue
CASP41

site_idAE2
Number of Residues5
Detailsbinding site for residue MPD C 304
ChainResidue
CTRP116
CGLY118
CALA136
CSER137
CHOH454

site_idAE3
Number of Residues6
Detailsbinding site for residue EDO C 305
ChainResidue
BSER193
BSER194
CARG79
CTRP82
CARG100
CHOH485

site_idAE4
Number of Residues5
Detailsbinding site for residue PO4 C 306
ChainResidue
CGLU120
CARG138
CHOH402
CHOH411
CHOH414

Functional Information from PROSITE/UniProt
site_idPS00101
Number of Residues29
DetailsHEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. IGteAmImpgVkIGhgAiIAsrSvVtkdV
ChainResidueDetails
AILE117-VAL145

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon