2O1W
Structure of N-terminal plus middle domains (N+M) of GRP94
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 |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006457 | biological_process | protein folding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
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 | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V |
| Chain | Residue | Details |
| A | ASN107 | |
| B | ASN107 | |
| C | ASN107 | |
| D | ASN107 | |
| E | ASN107 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V |
| Chain | Residue | Details |
| C | PHE199 | |
| D | ASP149 | |
| D | PHE199 | |
| E | ASP149 | |
| E | PHE199 | |
| A | ASP149 | |
| A | PHE199 | |
| B | ASP149 | |
| B | PHE199 | |
| C | ASP149 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V |
| Chain | Residue | Details |
| A | ASN162 | |
| B | ASN162 | |
| C | ASN162 | |
| D | ASN162 | |
| E | ASN162 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | SITE: Important for ATP hydrolysis => ECO:0000269|PubMed:17936703 |
| Chain | Residue | Details |
| A | ARG448 | |
| B | ARG448 | |
| C | ARG448 | |
| D | ARG448 | |
| E | ARG448 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P14625 |
| Chain | Residue | Details |
| A | LYS168 | |
| B | LYS168 | |
| C | LYS168 | |
| D | LYS168 | |
| E | LYS168 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HD0 |
| Chain | Residue | Details |
| C | SER403 | |
| D | SER172 | |
| D | SER403 | |
| E | SER172 | |
| E | SER403 | |
| A | SER172 | |
| A | SER403 | |
| B | SER172 | |
| B | SER403 | |
| C | SER172 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 5 |
| Details | MOD_RES: Phosphothreonine; by CK2 => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY288 | |
| B | GLY288 | |
| C | GLY288 | |
| D | GLY288 | |
| E | GLY288 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 5 |
| Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P14625, ECO:0000255 |
| Chain | Residue | Details |
| A | TRP343 | |
| B | TRP343 | |
| C | TRP343 | |
| D | TRP343 | |
| E | TRP343 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 5 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P08113 |
| Chain | Residue | Details |
| A | LYS404 | |
| B | LYS404 | |
| C | LYS404 | |
| D | LYS404 | |
| E | LYS404 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 5 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14625 |
| Chain | Residue | Details |
| A | SER447 | |
| B | SER447 | |
| C | SER447 | |
| D | SER447 | |
| E | SER447 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 5 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P08113 |
| Chain | Residue | Details |
| A | LYS479 | |
| B | LYS479 | |
| C | LYS479 | |
| D | LYS479 | |
| E | LYS479 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 25 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN107 | |
| B | ASN217 | |
| B | ASN445 | |
| B | ASN481 | |
| B | ASN502 | |
| C | ASN107 | |
| C | ASN217 | |
| C | ASN445 | |
| C | ASN481 | |
| C | ASN502 | |
| D | ASN107 | |
| D | ASN217 | |
| D | ASN445 | |
| D | ASN481 | |
| D | ASN502 | |
| E | ASN107 | |
| E | ASN217 | |
| E | ASN445 | |
| E | ASN481 | |
| E | ASN502 | |
| A | ASN107 | |
| A | ASN217 | |
| A | ASN445 | |
| A | ASN481 | |
| A | ASN502 |
