2O1V
Structure of full length GRP94 with ADP bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 755 |
| Chain | Residue |
| B | ASN107 |
| B | ADP302 |
| B | HOH860 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 755 |
| Chain | Residue |
| A | ASN107 |
| A | ADP301 |
| A | HOH891 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 756 |
| Chain | Residue |
| B | ASP737 |
| B | GLU740 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 756 |
| Chain | Residue |
| B | HOH836 |
| B | HOH837 |
| A | ASP737 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP A 301 |
| Chain | Residue |
| A | ASN107 |
| A | ALA111 |
| A | ASP149 |
| A | MET154 |
| A | ASN162 |
| A | GLY198 |
| A | PHE199 |
| A | MG755 |
| A | HOH776 |
| A | HOH891 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP B 302 |
| Chain | Residue |
| B | ASN107 |
| B | ALA111 |
| B | ASP149 |
| B | MET154 |
| B | ASN162 |
| B | GLY198 |
| B | PHE199 |
| B | THR245 |
| B | MG755 |
| B | HOH791 |
| B | HOH831 |
| B | HOH860 |
Functional Information from PROSITE/UniProt
| site_id | PS00298 |
| Number of Residues | 10 |
| Details | HSP90 Heat shock hsp90 proteins family signature. YkNKEIFLRE |
| Chain | Residue | Details |
| A | TYR94-GLU103 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15292259","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15951571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17936703","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TC0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15292259","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15951571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17936703","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TBW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15292259","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15951571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17936703","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TBW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for ATP hydrolysis","evidences":[{"source":"PubMed","id":"17936703","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14625","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P08113","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P08113","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 10 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
