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6R51

Crystal structure of apo PPEP-1(E143A/Y178F) in complex with fibrinogen-derived substrate peptide Ac-SLRPAPP-CONH2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0005576cellular_componentextracellular region
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008237molecular_functionmetallopeptidase activity
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue PO4 A 301
ChainResidue
AHIS25
ATYR194
AHOH402
AHOH412
AHOH425
AHOH471

site_idAC2
Number of Residues8
Detailsbinding site for Di-peptide ACE D 31 and SER D 32
ChainResidue
DLEU33
DARG34
DHOH101
FACE31
FSER32
AGLY117
AGLY118
ASER119

site_idAC3
Number of Residues10
Detailsbinding site for Di-peptide PRO D 37 and LPD D 38
ChainResidue
AGLY102
ATRP103
AHIS134
AASP135
AALA136
AHIS142
AASN175
APHE178
AHOH513
DALA36

site_idAC4
Number of Residues9
Detailsbinding site for Di-peptide ACE F 31 and SER F 32
ChainResidue
CGLY117
CGLY118
CSER119
CHIS150
DACE31
DSER32
FLEU33
FARG34
FHOH102

site_idAC5
Number of Residues8
Detailsbinding site for Di-peptide PRO F 37 and LPD F 38
ChainResidue
CGLY102
CTRP103
CHIS134
CASP135
CALA136
CHIS142
CPHE178
FALA36

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues555
DetailsDomain: {"description":"ATLF-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsRegion: {"description":"Interacts with substrate peptide","evidences":[{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24303041","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsSite: {"description":"Interacts with substrate peptide","evidences":[{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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