1EZR
CRYSTAL STRUCTURE OF NUCLEOSIDE HYDROLASE FROM LEISHMANIA MAJOR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0008477 | molecular_function | purine nucleosidase activity |
| A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| A | 0043101 | biological_process | purine-containing compound salvage |
| A | 0045437 | molecular_function | uridine nucleosidase activity |
| A | 0047724 | molecular_function | inosine nucleosidase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0008477 | molecular_function | purine nucleosidase activity |
| B | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| B | 0043101 | biological_process | purine-containing compound salvage |
| B | 0045437 | molecular_function | uridine nucleosidase activity |
| B | 0047724 | molecular_function | inosine nucleosidase activity |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0008477 | molecular_function | purine nucleosidase activity |
| C | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| C | 0043101 | biological_process | purine-containing compound salvage |
| C | 0045437 | molecular_function | uridine nucleosidase activity |
| C | 0047724 | molecular_function | inosine nucleosidase activity |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0008477 | molecular_function | purine nucleosidase activity |
| D | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| D | 0043101 | biological_process | purine-containing compound salvage |
| D | 0045437 | molecular_function | uridine nucleosidase activity |
| D | 0047724 | molecular_function | inosine nucleosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 401 |
| Chain | Residue |
| A | ASP10 |
| A | ASP15 |
| A | THR126 |
| A | ASP241 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 401 |
| Chain | Residue |
| B | ASP10 |
| B | ASP15 |
| B | THR126 |
| B | ASP241 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 401 |
| Chain | Residue |
| C | ASP15 |
| C | THR126 |
| C | ASP241 |
| C | ASP10 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 401 |
| Chain | Residue |
| D | ASP10 |
| D | ASP15 |
| D | THR126 |
| D | ASP241 |
Functional Information from PROSITE/UniProt
| site_id | PS01247 |
| Number of Residues | 11 |
| Details | IUNH Inosine-uridine preferring nucleoside hydrolase family signature. DcDPGiDDAVA |
| Chain | Residue | Details |
| A | ASP8-ALA18 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q27546","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mas |
| Chain | Residue | Details |
| A | ASP10 | |
| A | HIS240 | |
| A | ASN168 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mas |
| Chain | Residue | Details |
| B | ASP10 | |
| B | HIS240 | |
| B | ASN168 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mas |
| Chain | Residue | Details |
| C | ASP10 | |
| C | HIS240 | |
| C | ASN168 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mas |
| Chain | Residue | Details |
| D | ASP10 | |
| D | HIS240 | |
| D | ASN168 |
