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4Q1L

Crystal structure of Leucurolysin-a complexed with an endogenous tripeptide (QSW).

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0035821biological_processmodulation of process of another organism
A0042730biological_processfibrinolysis
A0046872molecular_functionmetal ion binding
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AGLU9
AASP93
ACYS197
AASN200
AHOH402
AHOH418

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
DTRP503
AHIS142
AHIS146
AHIS152

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 303
ChainResidue
AARG6
ASER72
AASN194
APRO195
AGLN196
AILE198
AHOH508

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AARG82
AHIS92
AASP93
ACYS117
AASP118
AARG151
ACYS197
AHOH407

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TMAHELGHNL
ChainResidueDetails
ATHR139-LEU148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AGLU143

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0007744|PDB:4Q1L
ChainResidueDetails
AGLU9
AASP93
AHIS142
AHIS146
AHIS152
ACYS197
AASN200

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:19652343
ChainResidueDetails
AGLN1

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PDB entries from 2025-01-08

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