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6WYN

Transition metal inhibition and structural refinement of the M. tuberculosis esterase, Rv0045c

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016787molecular_functionhydrolase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
A0106435molecular_functioncarboxylesterase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL A 401
ChainResidue
AGLY90
ASER154
ALEU155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21637775","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25354081","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"25354081","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"21637775","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25354081","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Involved in substrate selectivity","evidences":[{"source":"PubMed","id":"25354081","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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