Structure of PDB 5x9u Chain D

Receptor sequence
>5x9uD (length=494) Species: 246194 (Carboxydothermus hydrogenoformans Z-2901) [Search protein sequence]
EIEERYQALFSNAAAVKALTQVVANSLGPKGLDAMLVDRFGEVVVTNDGV
TILTLMDAQHPAARMVVNMARAQEREVGDGTTTAAVLAGALVSEGVNQIL
KGVPVSKVLAGMNRALNHALFLIRKNAIKVGSITDDRLLAAAKIAGRGDE
RVAAILRDAAAMLEDKLQDPGFKLADLVLAKVGADTTLIPGVVINKSPLW
EEGSQKLQEVRLLVLDDGLYPEEVEEEALASEAGFEQYLKNQKIFQENLK
KLKELGVKLILLTRGISDIAEEFCYENEIMVITRITQKELKRVLEFTGAR
AAKRTSLNKPVEELQKMLGYARTCFYDSRLDFTIIEGGAGKATATVLIGA
ATDEVVDEQERIAKDAAGSFAAAYRSGVLPGGGAFFLYLSREVESLKNRL
PGMESYGVMAFSEALKVPFRVMAENAGFNGLEKLGDLMTLQVQKNNYALG
LDFETGEFIDMIAGGVVDPAEVVYQAVKNASEVAISLLKINTII
3D structure
PDB5x9u Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium
ChainD
Resolution4.001 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D56 T89 T90 D373
Catalytic site (residue number reindexed from 1) D48 T81 T82 D365
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP D P37 D87 G88 T89 T90 T91 G389 G390 M430 V474 D476 P29 D79 G80 T81 T82 T83 G381 G382 M422 V466 D468
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

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Molecular Function
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Biological Process
External links
PDB RCSB:5x9u, PDBe:5x9u, PDBj:5x9u
PDBsum5x9u
PubMed29018216
UniProtQ3AF10

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