Structure of PDB 5w74 Chain A

Receptor sequence
>5w74A (length=477) Species: 39152 (Methanococcus maripaludis) [Search protein sequence]
DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREM
SVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPT
IVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKE
KLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKER
VSAQMPKKVTDAKIALLNCAIEMLKDMVAEIKASGANVLFCQKGIDDLAQ
HYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEE
RKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDAAVGVVGCTI
EDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLA
ENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVK
TQAIQSAAESTEMLLRIDDVIAAEKLR
3D structure
PDB5w74 The Conformational Cycle of the Group II Chaperonin Termini
ChainA
Resolution3.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D60 T93 T94 A386
Catalytic site (residue number reindexed from 1) D42 T75 T76 A341
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 A L39 G40 D91 G92 G160 G403 G404 L473 N474 V488 E490 L21 G22 D73 G74 G142 G358 G359 L428 N429 V443 E445
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:5w74, PDBe:5w74, PDBj:5w74
PDBsum5w74
PubMed
UniProtQ877G8

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