Structure of PDB 4xcd Chain E

Receptor sequence

>4xcdE (length=501) Species: 273057 (Saccharolobus solfataricus P2)

YGKEALRANIAAVKAIEEALKSTYGPRGMDKMLVDSLGDITITNDGATIL
DKMDLQHPTGKLLVQIAKGQDEETADGTKTAVILAGELAKKAEDLLYKEI
HPTIIVSGYKKAEEIALKTIQEIAQPVTINDTDVLRKVALTSLGSKAVAG
AREYLADLVVKAVAQVAELRGDKWYVDLDNVQIVKKHGGSVNDTQLVYGI
VVDKEVVHPGMPKRIENAKIALLDASVEKPELDAEIRIQMHKFLEEEENI
LKEKVDKIAATGNVVICQKGIDEVAQHYLAKKGILAVRRAKKSDLEKLAR
ATGGRVISNIDELTSQDLGYAALVEERKVGEDKMVFVEGAKNPKSVSILI
RGGLERVVDETERALRDALGTVADVIRDGRAVAGGGAVEIEIAKRLRKYA
PQVGGKEQLAIEAYANAIEGLIMILAENAGLDPIDKLMQLRSLHENETNK
WYGLNLFTGNPEDMWKLGVIEPALVKMNAVKAATEAVTLVLRIDDIVAAG
K

3D structure

• PDB: 4xcd Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins.
• Chain: E
• Resolution: 3.79 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D73 T106 K107 D402
• Catalytic site (residue number reindexed from 1): D45 T78 K79 D367

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	E	Y52 P54 D104 G105 K107 T108 S173 G419 G420 L491 E506	Y24 P26 D76 G77 K79 T80 S145 G384 G385 L456 E471

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0016887 ATP hydrolysis activity
• GO:0042802 identical protein binding
• GO:0051082 unfolded protein binding
• GO:0140662 ATP-dependent protein folding chaperone

Biological Process

• GO:0006457 protein folding

External links

• PDB: RCSB:4xcd, PDBe:4xcd, PDBj:4xcd
• PDBsum: 4xcd
• PubMed: 26853941
• UniProt: Q9V2T8|THSB_SACS2 Thermosome subunit beta (Gene Name=thsB)