5EVZ
Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ADP and inorganic phosphate
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 501 |
| Chain | Residue |
| A | PO4502 |
| A | ADP503 |
| A | HOH622 |
| A | HOH653 |
| A | HOH673 |
| A | HOH692 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue PO4 A 502 |
| Chain | Residue |
| A | PRO173 |
| A | GLU201 |
| A | THR229 |
| A | MG501 |
| A | ADP503 |
| A | HOH603 |
| A | HOH622 |
| A | HOH639 |
| A | HOH653 |
| A | HOH692 |
| A | GLY36 |
| A | THR37 |
| A | LYS96 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue ADP A 503 |
| Chain | Residue |
| A | THR37 |
| A | THR38 |
| A | TYR39 |
| A | GLY226 |
| A | GLY227 |
| A | GLY255 |
| A | GLU293 |
| A | LYS296 |
| A | ARG297 |
| A | SER300 |
| A | GLY363 |
| A | GLY364 |
| A | SER365 |
| A | ARG367 |
| A | ILE368 |
| A | ASP391 |
| A | MG501 |
| A | PO4502 |
| A | HOH602 |
| A | HOH603 |
| A | HOH606 |
| A | HOH622 |
| A | HOH673 |
| A | HOH692 |
| A | HOH696 |
| A | HOH721 |
| A | HOH740 |
| A | HOH746 |
| A | HOH848 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue PO4 B 501 |
| Chain | Residue |
| B | GLY36 |
| B | THR37 |
| B | LYS96 |
| B | GLU201 |
| B | THR229 |
| B | MG502 |
| B | ADP503 |
| B | HOH601 |
| B | HOH614 |
| B | HOH622 |
| B | HOH654 |
| B | HOH666 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | PO4501 |
| B | ADP503 |
| B | HOH614 |
| B | HOH622 |
| B | HOH654 |
| B | HOH669 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | binding site for residue ADP B 503 |
| Chain | Residue |
| B | THR37 |
| B | THR38 |
| B | TYR39 |
| B | GLY226 |
| B | GLY227 |
| B | GLY255 |
| B | GLU293 |
| B | LYS296 |
| B | ARG297 |
| B | SER300 |
| B | GLY363 |
| B | GLY364 |
| B | SER365 |
| B | ARG367 |
| B | ILE368 |
| B | ASP391 |
| B | PO4501 |
| B | MG502 |
| B | HOH601 |
| B | HOH603 |
| B | HOH622 |
| B | HOH654 |
| B | HOH659 |
| B | HOH662 |
| B | HOH669 |
| B | HOH679 |
| B | HOH700 |
| B | HOH718 |
Functional Information from PROSITE/UniProt
| site_id | PS00297 |
| Number of Residues | 8 |
| Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS |
| Chain | Residue | Details |
| A | ILE33-SER40 |
| site_id | PS00329 |
| Number of Residues | 14 |
| Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGTfdvSLL |
| Chain | Residue | Details |
| A | VAL222-LEU235 |
| site_id | PS01036 |
| Number of Residues | 15 |
| Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ |
| Chain | Residue | Details |
| A | ILE359-GLN373 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 310 |
| Details | Region: {"description":"Nucleotide-binding (NBD)","evidences":[{"source":"PubMed","id":"28286085","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21526763","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06761","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DMV8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
