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1CLA

EVIDENCE FOR TRANSITION-STATE STABILIZATION BY SERINE-148 IN THE CATALYTIC MECHANISM OF CHLORAMPHENICOL ACETYLTRANSFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0008811molecular_functionchloramphenicol O-acetyltransferase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 222
ChainResidue
AGLU23
AGLU23
AHIS27
AHIS27

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 223
ChainResidue
AHOH282
AHOH282
AHOH341
AHOH341

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CLM A 221
ChainResidue
ALEU29
AALA105
APHE135
ALEU160
AVAL162
ATYR168
AHIS195
AHOH249
AHOH252
AHOH308
AHOH313
AHOH320
ATYR25

Functional Information from PROSITE/UniProt
site_idPS00100
Number of Residues11
DetailsCAT Chloramphenicol acetyltransferase active site. QVHHAvcDGFH
ChainResidueDetails
AGLN192-HIS202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 3cla
ChainResidueDetails
AASP199
AHIS195
AARG18

site_idMCSA1
Number of Residues4
DetailsM-CSA 934
ChainResidueDetails
AARG18electrostatic stabiliser
ATHR174activator, transition state stabiliser
AHIS195proton shuttle (general acid/base)
AASP199electrostatic stabiliser, modifies pKa

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PDB entries from 2025-07-30

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