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1LM4

Structure of Peptide Deformylase from Staphylococcus aureus at 1.45 A

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 Residues4
DetailsBINDING SITE FOR RESIDUE FE A 603
ChainResidue
AGLY-10
AOCS111
AHIS154
AHIS158

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 603
ChainResidue
BGLN65
BOCS111
BHIS154
BHIS158
BHOH616

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 601
ChainResidue
BGLU109
BGLY110
BTYR147
BHIS154
BHOH687
BHOH784
BHOH866

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AGLU155
BGLU155

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AOCS111
AHIS154
AHIS158
BOCS111
BHIS154
BHIS158

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bs4
ChainResidueDetails
AGLU155
AGLY60
ALEU112
AGLN65

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bs4
ChainResidueDetails
BGLU155
BGLY60
BLEU112
BGLN65

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PDB entries from 2024-07-17

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