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6OFT

The crystal structure of the first half of the periplasmic protease PqqL from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0046872molecular_functionmetal ion binding
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 1001
ChainResidue
ATYR287
AARG451
ATRP458
ALEU478
AGLU481

site_idAC2
Number of Residues7
Detailsbinding site for residue PO4 A 1002
ChainResidue
AGLN399
AARG402
AHOH1129
ALYS34
ATYR49
APRO50
AHIS51

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 1003
ChainResidue
AHIS267
ALEU268

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 1004
ChainResidue
AGLU196
APRO197
AILE198

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL B 1001
ChainResidue
BTYR287
BARG451
BTRP458
BLEU478
BGLU481

site_idAC6
Number of Residues6
Detailsbinding site for residue PO4 B 1002
ChainResidue
BLYS34
BTYR49
BPRO50
BHIS51
BGLN399
BARG402

Functional Information from PROSITE/UniProt
site_idPS00143
Number of Residues24
DetailsINSULINASE Insulinase family, zinc-binding region signature. GslqeednelGvAHFVEHMmFnGT
ChainResidueDetails
AGLY67-THR90

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10096","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10096","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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