2H8M
N-Domain Of Grp94 In Complex With the 2-Iodo-NECA
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 | 12 |
| Details | BINDING SITE FOR RESIDUE NEI A 401 |
| Chain | Residue |
| A | ALA111 |
| A | HOH524 |
| A | HOH631 |
| A | HOH689 |
| A | ASP149 |
| A | VAL152 |
| A | GLY153 |
| A | MET154 |
| A | ASN162 |
| A | LEU163 |
| A | PHE199 |
| A | HOH522 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NEI B 402 |
| Chain | Residue |
| B | ALA111 |
| B | ASP149 |
| B | VAL152 |
| B | GLY153 |
| B | MET154 |
| B | ASN162 |
| B | LEU163 |
| B | PHE199 |
| B | HOH604 |
| B | HOH605 |
| B | HOH607 |
| B | HOH608 |
| B | HOH693 |
| B | HOH699 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 B 501 |
| Chain | Residue |
| B | THR212 |
| B | ARG237 |
| B | HOH675 |
| B | HOH720 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 B 502 |
| Chain | Residue |
| B | LYS137 |
| B | HIS146 |
| B | THR148 |
| B | LEU241 |
| B | HOH708 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PG4 A 504 |
| Chain | Residue |
| A | THR212 |
| A | ARG237 |
| A | THR240 |
| A | THR248 |
| A | HOH534 |
| A | HOH554 |
| A | HOH585 |
| A | HOH651 |
| A | HOH686 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 A 505 |
| Chain | Residue |
| A | LYS137 |
| A | HIS146 |
| A | TRP282 |
| A | HOH590 |
| A | HOH597 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PG4 A 506 |
| Chain | Residue |
| A | ASN162 |
| A | HOH668 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 A 507 |
| Chain | Residue |
| A | ASP110 |
| A | ASP113 |
| A | LYS114 |
| A | LEU117 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 508 |
| Chain | Residue |
| B | ASN107 |
| B | ALA108 |
| B | ASP149 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 B 509 |
| Chain | Residue |
| B | ASP110 |
| B | LYS114 |
| B | LEU117 |
| B | HOH711 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PG4 A 510 |
| Chain | Residue |
| A | THR263 |
| A | ASN266 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1PE B 601 |
| Chain | Residue |
| A | ASN83 |
| A | LYS87 |
| A | ILE90 |
| A | SER227 |
| B | ASN83 |
| B | LYS87 |
| B | ILE90 |
| B | SER227 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE B 602 |
| Chain | Residue |
| A | LYS75 |
| A | ALA77 |
| A | PHE78 |
| B | LYS75 |
| B | PHE76 |
| B | ALA77 |
| B | HOH724 |
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 | 1 |
| 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 |
