1YSZ
Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH NECA
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NEC A 338 |
| Chain | Residue |
| A | ALA111 |
| A | HOH346 |
| A | HOH351 |
| A | HOH360 |
| A | HOH374 |
| A | HOH377 |
| A | HOH394 |
| A | ASP149 |
| A | MET154 |
| A | ASN162 |
| A | LEU163 |
| A | GLY196 |
| A | PHE199 |
| A | TYR200 |
| A | HOH342 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 A 339 |
| Chain | Residue |
| A | LEU117 |
| A | THR212 |
| A | ARG237 |
| A | THR248 |
| A | PG4340 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 A 340 |
| Chain | Residue |
| A | LYS137 |
| A | THR148 |
| A | TRP282 |
| A | PG4339 |
| A | HOH395 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 A 341 |
| Chain | Residue |
| A | ASN83 |
| A | LYS87 |
| A | ILE90 |
| A | SER227 |
| A | HOH364 |
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 | 1 |
| 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 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| 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 |
| A | ASP149 | |
| A | PHE199 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P14625 |
| Chain | Residue | Details |
| A | LYS168 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HD0 |
| Chain | Residue | Details |
| A | SER172 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CK2 => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY325 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P14625, ECO:0000255 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN107 | |
| A | ASN217 |
