1LML
LEISHMANOLYSIN
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 578 |
| Chain | Residue |
| A | GLU265 |
| A | HIS268 |
| A | HIS334 |
| A | HOH663 |
| A | HIS264 |
| site_id | ACT |
| Number of Residues | 5 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| A | HIS264 |
| A | GLU265 |
| A | HIS268 |
| A | HIS334 |
| A | MET345 |
| site_id | CA1 |
| Number of Residues | 1 |
| Details | CARBOHYDRATE BINDING SITE. |
| Chain | Residue |
| A | ASN300 |
| site_id | CA2 |
| Number of Residues | 1 |
| Details | CARBOHYDRATE BINDING SITE. |
| Chain | Residue |
| A | ASN407 |
| site_id | CA3 |
| Number of Residues | 1 |
| Details | CARBOHYDRATE BINDING SITE. |
| Chain | Residue |
| A | ASN534 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVTHEMAHAL |
| Chain | Residue | Details |
| A | VAL261-LEU270 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9739094","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9739094","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7675788","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9041519","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"7675788","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 8519803, 9739094 |
| Chain | Residue | Details |
| A | GLU265 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 668 |
| Chain | Residue | Details |
| A | HIS264 | metal ligand |
| A | GLU265 | proton shuttle (general acid/base) |
| A | HIS268 | metal ligand |
| A | HIS334 | metal ligand |
