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Atomic model of bovine tric CCT2(BETA) subunit derived from a 4.0 ångström cryo-EM MAP

Analyse Atomic model of bovine tric CCT2(BETA) subunit derived from a 4.0 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KTT
Type: protein
Length: 513 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T-complex protein 1 subunit beta
UniProt: Q3ZBH0
Pockets: 4 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	T-complex protein 1 subunit beta	protein	513	48% helix, 13% strand	Q3ZBH0

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	973	0.85	0.86	150	empty
2	265	0.66	0.83	53	empty
3	258	0.62	0.81	32	empty
4	53	0.28	0.75	20	empty

Compared structures

3KTT · Atomic model of bovine TRiC CCT2(beta) subunit derived from a 4.0 Angstrom cryo-EM map · the same entry in another collection · chain B against B, TM-score 1.00
Q3ZBH0 · AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit beta (Q3ZBH0) · a predicted model of the same protein · chain B against A, TM-score 0.92

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q3ZBH0
Elsewhere: RCSB PDB 3KTT · PDBe 3KTT · UniProt Q3ZBH0

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