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3LQ0

Zymogen structure of crayfish astacin metallopeptidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0007155biological_processcell adhesion
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0009566biological_processfertilization
A0010954biological_processpositive regulation of protein processing
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0060468biological_processprevention of polyspermy
A0060473cellular_componentcortical granule
A0070001molecular_functionaspartic-type peptidase activity
A0070002molecular_functionglutamic-type peptidase activity
A2000360biological_processnegative regulation of binding of sperm to zona pellucida
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 999
ChainResidue
AASP21
AHIS92
AHIS96
AHIS102
ATYR149

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AHOH540
AHOH543
AHOH706
AHOH771
AALA7
ATYR86
ATYR177
AHOH516

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
ALEU31
AGLU38
APHE45
AHOH511
AHOH520
AHOH719
AHOH733

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
ATYR54
AGLU56
AALA74
AARG135
AHOH606

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
ASER23
AGLY24
ALYS151
ATYR152
AASP172
AHOH695

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues33
DetailsPropeptide: {"description":"Activation peptide","featureId":"PRO_0000028872","evidences":[{"source":"PubMed","id":"3548817","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues198
DetailsDomain: {"description":"Peptidase M12A","evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1319561","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1319561","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8756323","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 403
ChainResidueDetails
AHIS92metal ligand
AALA93proton shuttle (general acid/base)
AHIS96metal ligand
AHIS102metal ligand
ATYR149transition state stabiliser

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PDB entries from 2025-12-03

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