1YT1
Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL
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 | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 A 501 |
| Chain | Residue |
| A | THR212 |
| A | ARG237 |
| A | THR240 |
| A | THR248 |
| A | HOH614 |
| A | HOH657 |
| A | HOH682 |
| A | HOH702 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 A 502 |
| Chain | Residue |
| A | HIS146 |
| A | TRP282 |
| A | HOH603 |
| A | HOH672 |
| A | HOH684 |
| A | LYS137 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 A 503 |
| Chain | Residue |
| A | ALA111 |
| A | ASP149 |
| A | MET154 |
| A | HOH505 |
| A | HOH595 |
| A | HOH683 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 A 504 |
| Chain | Residue |
| A | ASP110 |
| A | LYS114 |
| A | HOH592 |
| A | HOH594 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PG4 B 508 |
| Chain | Residue |
| B | THR212 |
| B | ARG237 |
| B | THR248 |
| B | PG4509 |
| B | HOH621 |
| B | HOH662 |
| B | HOH710 |
| B | HOH804 |
| B | HOH817 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 B 509 |
| Chain | Residue |
| B | LYS137 |
| B | THR148 |
| B | PG4508 |
| B | HOH667 |
| B | HOH675 |
| B | HOH792 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 511 |
| Chain | Residue |
| B | ASN129 |
| B | ASN239 |
| B | GLY242 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 B 512 |
| Chain | Residue |
| B | ASP262 |
| B | THR263 |
| B | ASN266 |
| B | HOH712 |
| B | HOH797 |
| B | HOH824 |
| B | HOH833 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PE B 606 |
| Chain | Residue |
| A | ASN83 |
| A | LYS87 |
| A | ILE90 |
| A | SER227 |
| B | ASN83 |
| B | LYS87 |
| B | ILE90 |
| B | SER227 |
| B | HOH670 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 B 613 |
| Chain | Residue |
| B | ASN107 |
| B | ALA111 |
| B | ASP149 |
| B | MET154 |
| B | HOH617 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 614 |
| Chain | Residue |
| B | ASP110 |
| B | LYS114 |
| B | PG4615 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 615 |
| Chain | Residue |
| B | LYS114 |
| B | PG4614 |
| B | HOH755 |
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 | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q66HD0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P14625","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
