4JN4
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006260 | biological_process | DNA replication |
| A | 0006457 | biological_process | protein folding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009408 | biological_process | response to heat |
| A | 0016020 | cellular_component | membrane |
| A | 0016234 | cellular_component | inclusion body |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0016989 | molecular_function | sigma factor antagonist activity |
| A | 0031072 | molecular_function | heat shock protein binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0034620 | biological_process | cellular response to unfolded protein |
| A | 0042026 | biological_process | protein refolding |
| A | 0043335 | biological_process | protein unfolding |
| A | 0043531 | molecular_function | ADP binding |
| A | 0044183 | molecular_function | protein folding chaperone |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| A | 0065003 | biological_process | protein-containing complex assembly |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| A | 1990169 | biological_process | stress response to copper ion |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006260 | biological_process | DNA replication |
| B | 0006457 | biological_process | protein folding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009408 | biological_process | response to heat |
| B | 0016020 | cellular_component | membrane |
| B | 0016234 | cellular_component | inclusion body |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0016989 | molecular_function | sigma factor antagonist activity |
| B | 0031072 | molecular_function | heat shock protein binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0034620 | biological_process | cellular response to unfolded protein |
| B | 0042026 | biological_process | protein refolding |
| B | 0043335 | biological_process | protein unfolding |
| B | 0043531 | molecular_function | ADP binding |
| B | 0044183 | molecular_function | protein folding chaperone |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0065003 | biological_process | protein-containing complex assembly |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 1990169 | biological_process | stress response to copper ion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1001 |
| Chain | Residue |
| A | ATP1002 |
| A | HOH1101 |
| A | HOH1103 |
| A | HOH1439 |
| A | HOH1573 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE ATP A 1002 |
| Chain | Residue |
| A | LYS70 |
| A | GLY196 |
| A | GLY197 |
| A | GLY198 |
| A | ALA199 |
| A | GLY229 |
| A | GLU267 |
| A | LYS270 |
| A | ILE271 |
| A | SER274 |
| A | GLY341 |
| A | GLY342 |
| A | GLN343 |
| A | ARG345 |
| A | MG1001 |
| A | HOH1101 |
| A | HOH1103 |
| A | HOH1105 |
| A | HOH1108 |
| A | HOH1115 |
| A | HOH1119 |
| A | HOH1173 |
| A | HOH1181 |
| A | HOH1247 |
| A | HOH1439 |
| A | HOH1573 |
| B | HOH1196 |
| A | GLY10 |
| A | THR11 |
| A | THR12 |
| A | ASN13 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
| Chain | Residue |
| A | ARG25 |
| A | ARG34 |
| A | GOL1008 |
| A | HOH1163 |
| A | HOH1329 |
| B | ASN366 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
| Chain | Residue |
| A | ARG445 |
| A | LYS446 |
| A | HOH1189 |
| A | HOH1511 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1005 |
| Chain | Residue |
| A | ARG188 |
| A | ARG362 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1006 |
| Chain | Residue |
| A | SER427 |
| A | MET428 |
| A | GLY429 |
| A | GLY430 |
| A | HOH1425 |
| B | MET428 |
| B | SO41006 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1007 |
| Chain | Residue |
| A | ARG467 |
| A | SER545 |
| A | LYS548 |
| B | VAL407 |
| B | ARG447 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1008 |
| Chain | Residue |
| A | ARG25 |
| A | VAL26 |
| A | LEU27 |
| A | GLU28 |
| A | SO41003 |
| B | ASN366 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1009 |
| Chain | Residue |
| A | ARG84 |
| A | ARG235 |
| A | ARG315 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1001 |
| Chain | Residue |
| B | ATP1002 |
| B | HOH1101 |
| B | HOH1102 |
| B | HOH1347 |
| B | HOH1432 |
| site_id | BC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ATP B 1002 |
| Chain | Residue |
| B | HOH1135 |
| B | HOH1139 |
| B | HOH1191 |
| B | HOH1347 |
| B | HOH1432 |
| A | HOH1147 |
| B | GLY10 |
| B | THR11 |
| B | THR12 |
| B | ASN13 |
| B | LYS70 |
| B | GLY196 |
| B | GLY197 |
| B | GLY198 |
| B | ALA199 |
| B | GLY229 |
| B | GLU267 |
| B | LYS270 |
| B | SER274 |
| B | GLY341 |
| B | GLY342 |
| B | GLN343 |
| B | ARG345 |
| B | MG1001 |
| B | HOH1101 |
| B | HOH1102 |
| B | HOH1105 |
| B | HOH1109 |
| B | HOH1111 |
| B | HOH1120 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1003 |
| Chain | Residue |
| A | ASN366 |
| B | ARG25 |
| B | ARG34 |
| B | GOL1009 |
| B | HOH1383 |
| B | HOH1407 |
| B | HOH1605 |
| B | HOH1646 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1004 |
| Chain | Residue |
| A | LYS268 |
| B | ARG56 |
| B | HOH1455 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1005 |
| Chain | Residue |
| B | ARG188 |
| B | ARG362 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1006 |
| Chain | Residue |
| A | MET428 |
| A | SO41006 |
| B | SER427 |
| B | MET428 |
| B | GLY429 |
| B | GLY430 |
| B | HOH1633 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1007 |
| Chain | Residue |
| A | VAL407 |
| A | ARG447 |
| B | ARG467 |
| B | SER545 |
| B | LYS548 |
| B | HOH1494 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1008 |
| Chain | Residue |
| A | HOH1438 |
| B | ARG445 |
| B | LYS446 |
| B | ARG447 |
| B | HOH1165 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1009 |
| Chain | Residue |
| A | ASN366 |
| A | HOH1225 |
| B | ARG25 |
| B | VAL26 |
| B | GLU28 |
| B | ARG34 |
| B | TYR130 |
| B | SO41003 |
| B | HOH1167 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1010 |
| Chain | Residue |
| B | ASP231 |
| B | ARG235 |
| B | ARG315 |
| B | HOH1451 |
| B | HOH1588 |
Functional Information from PROSITE/UniProt
| site_id | PS00297 |
| Number of Residues | 8 |
| Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS |
| Chain | Residue | Details |
| A | ILE7-SER14 |
| site_id | PS00329 |
| Number of Residues | 14 |
| Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGAfdiSII |
| Chain | Residue | Details |
| A | VAL192-ILE205 |
| site_id | PS01036 |
| Number of Residues | 15 |
| Details | HSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGqTRMPmVqK |
| Chain | Residue | Details |
| A | VAL337-LYS351 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"1835085","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8206983","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
