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1LML

LEISHMANOLYSIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0007155biological_processcell adhesion
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 578
ChainResidue
AGLU265
AHIS268
AHIS334
AHOH663
AHIS264

site_idACT
Number of Residues5
DetailsACTIVE SITE.
ChainResidue
AHIS264
AGLU265
AHIS268
AHIS334
AMET345

site_idCA1
Number of Residues1
DetailsCARBOHYDRATE BINDING SITE.
ChainResidue
AASN300

site_idCA2
Number of Residues1
DetailsCARBOHYDRATE BINDING SITE.
ChainResidue
AASN407

site_idCA3
Number of Residues1
DetailsCARBOHYDRATE BINDING SITE.
ChainResidue
AASN534

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVTHEMAHAL
ChainResidueDetails
AVAL261-LEU270

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:9739094
ChainResidueDetails
AGLU265

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:9739094
ChainResidueDetails
AHIS264
AHIS268
AHIS334

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: GPI-anchor amidated asparagine => ECO:0000269|PubMed:2145267
ChainResidueDetails
AASN577

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:7675788, ECO:0000269|PubMed:9041519
ChainResidueDetails
AASN300
AASN407

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:7675788
ChainResidueDetails
AASN534

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 8519803, 9739094
ChainResidueDetails
AGLU265

site_idMCSA1
Number of Residues4
DetailsM-CSA 668
ChainResidueDetails
AHIS264metal ligand
AGLU265proton shuttle (general acid/base)
AHIS268metal ligand
AHIS334metal ligand

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PDB entries from 2024-07-10

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