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6JEU

K1U bound crystal peptide deformylase from Acinetobacter baumanii

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 PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 201
ChainResidue
AGLN51
ACYS92
AHIS134
AHIS138
AK1U202

site_idAC2
Number of Residues14
Detailsbinding site for residue K1U A 202
ChainResidue
ATYR88
AGLU90
AGLY91
ACYS92
ALEU93
ATYR99
AHIS134
AGLU135
AHIS138
AZN201
AGLY44
AILE45
AGLY46
AGLN51

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 201
ChainResidue
BCYS92
BHIS134
BHIS138
BK1U202

site_idAC4
Number of Residues14
Detailsbinding site for residue K1U B 202
ChainResidue
BGLY44
BILE45
BGLY46
BGLN51
BTYR88
BGLU90
BGLY91
BCYS92
BLEU93
BTYR99
BHIS134
BGLU135
BHIS138
BZN201

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

249697

PDB entries from 2026-02-25

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