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1LME

Crystal Structure of Peptide Deformylase from Thermotoga maritima

Functional Information from GO Data
ChainGOidnamespacecontents
A0006412biological_processtranslation
A0016787molecular_functionhydrolase activity
A0042586molecular_functionpeptide deformylase activity
A0046872molecular_functionmetal ion binding
B0006412biological_processtranslation
B0016787molecular_functionhydrolase activity
B0042586molecular_functionpeptide deformylase activity
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00163","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00163","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bs4
ChainResidueDetails
AGLY44
AGLN49
ALEU88
AGLU130

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bs4
ChainResidueDetails
BGLY44
BGLN49
BLEU88
BGLU130

243531

PDB entries from 2025-10-22

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