5WMT
Structure of GRP94 N-terminal Domain bound to resorcinylic inhibitor BnIm.
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 |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006457 | biological_process | protein folding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0051082 | molecular_function | unfolded protein binding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 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 EDO A 401 |
| Chain | Residue |
| A | HIS221 |
| A | HOH504 |
| C | LYS208 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | LYS214 |
| A | ASN216 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | LYS135 |
| A | TRP333 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | LYS135 |
| A | TYR280 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue 9QY A 405 |
| Chain | Residue |
| A | ASN107 |
| A | ALA111 |
| A | ASP149 |
| A | MET154 |
| A | ASN162 |
| A | PHE195 |
| A | THR245 |
| A | ILE247 |
| A | HOH501 |
| A | HOH503 |
| A | HOH507 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 401 |
| Chain | Residue |
| B | SER169 |
| B | LYS208 |
| B | GLU224 |
| B | ASP226 |
| B | GLU229 |
| B | PHE230 |
| B | SER231 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | ARG156 |
| B | HIS221 |
| D | LYS208 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | THR212 |
| B | ARG237 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 404 |
| Chain | Residue |
| B | TRP282 |
| B | TRP331 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue 9QY B 405 |
| Chain | Residue |
| B | ASN107 |
| B | ALA111 |
| B | ASP149 |
| B | MET154 |
| B | ASN162 |
| B | PHE195 |
| B | TRP223 |
| B | ILE247 |
| B | HOH502 |
| B | HOH504 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 401 |
| Chain | Residue |
| C | SER169 |
| C | LYS208 |
| C | GLU224 |
| C | ASP226 |
| C | GLU229 |
| C | PHE230 |
| C | SER231 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 402 |
| Chain | Residue |
| C | THR212 |
| C | ARG237 |
| C | EDO403 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 403 |
| Chain | Residue |
| C | EDO402 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 404 |
| Chain | Residue |
| A | LYS208 |
| C | THR219 |
| C | HIS221 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue MG C 405 |
| Chain | Residue |
| C | TRP282 |
| C | TRP331 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue 9QY C 406 |
| Chain | Residue |
| C | ALA111 |
| C | ASP149 |
| C | MET154 |
| C | ASN162 |
| C | LEU163 |
| C | PHE195 |
| C | TRP223 |
| C | ILE247 |
| C | HOH503 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 401 |
| Chain | Residue |
| B | LYS208 |
| D | HIS221 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 402 |
| Chain | Residue |
| D | LYS135 |
| D | TRP333 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 403 |
| Chain | Residue |
| D | LYS214 |
| D | ASN216 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 404 |
| Chain | Residue |
| B | VAL250 |
| D | THR219 |
| D | ALA234 |
| D | ASP235 |
| D | GLY238 |
| site_id | AE3 |
| Number of Residues | 12 |
| Details | binding site for residue 9QY D 405 |
| Chain | Residue |
| D | ASN107 |
| D | ALA111 |
| D | ASP149 |
| D | MET154 |
| D | ASN162 |
| D | LEU163 |
| D | PHE195 |
| D | THR245 |
| D | ILE247 |
| D | HOH502 |
| D | HOH505 |
| D | HOH507 |
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 | 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":"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 | 8 |
| 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 | 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":"2O1U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P14625","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q66HD0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
