4JN4
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0051085 | biological_process | chaperone cofactor-dependent protein refolding |
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 | 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 | 0051085 | biological_process | chaperone cofactor-dependent protein refolding |
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 | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
A | LYS70 | |
B | GLY506 | |
B | LEU532 | |
B | LEU591 | |
A | LYS246 | |
A | LYS359 | |
A | GLY506 | |
A | LEU532 | |
A | LEU591 | |
B | LYS70 | |
B | LYS246 | |
B | LYS359 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS109 | |
A | LYS421 | |
A | ASP560 | |
B | LYS109 | |
B | LYS421 | |
B | ASP560 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:1835085, ECO:0000269|PubMed:8206983 |
Chain | Residue | Details |
A | ALA199 | |
B | ALA199 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
A | LYS245 | |
A | LYS304 | |
B | LYS245 | |
B | LYS304 |