1QYE
Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CDY A 338 |
Chain | Residue |
A | ASN107 |
A | HOH343 |
A | HOH347 |
A | HOH358 |
A | HOH390 |
A | HOH429 |
A | ALA111 |
A | ASP149 |
A | VAL152 |
A | GLY153 |
A | MET154 |
A | ASN162 |
A | LEU163 |
A | PHE199 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE M2M A 339 |
Chain | Residue |
A | ASN83 |
A | LYS87 |
A | LYS87 |
A | ILE90 |
A | SER227 |
A | HOH478 |
A | HOH522 |
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 | THR288 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P14625, ECO:0000255 |
Chain | Residue | Details |
A | SER306 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN107 | |
A | ASN217 |