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6IZI

Crystal structure of E. coli peptide deformylase and methionine aminopeptidase fitted into the cryo-EM density map of the complex

Functional Information from GO Data
ChainGOidnamespacecontents
P0005515molecular_functionprotein binding
P0005829cellular_componentcytosol
P0006412biological_processtranslation
P0008198molecular_functionferrous iron binding
P0008270molecular_functionzinc ion binding
P0016787molecular_functionhydrolase activity
P0031365biological_processN-terminal protein amino acid modification
P0042586molecular_functionpeptide deformylase activity
P0043022molecular_functionribosome binding
P0046872molecular_functionmetal ion binding
Q0004177molecular_functionaminopeptidase activity
Q0004239molecular_functioninitiator methionyl aminopeptidase activity
Q0005506molecular_functioniron ion binding
Q0005829cellular_componentcytosol
Q0006508biological_processproteolysis
Q0008198molecular_functionferrous iron binding
Q0008233molecular_functionpeptidase activity
Q0016787molecular_functionhydrolase activity
Q0046872molecular_functionmetal ion binding
Q0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIGqgfHeepqVl.HY
ChainResidueDetails
QTYR168-TYR186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"9846875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9846875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10387007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18093325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18785729","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails

246905

PDB entries from 2025-12-31

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