MolNFT v1 · #36060 · protein

Crystal structure of the chaperonin groel-E461K

2EU1: “Crystal structure of the chaperonin groel-E461K”. X-ray diffraction, 20 pockets (best druggability 0.81). MolNFT v1 #36060 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2EU1
Type: protein
Length: 7,336 residues
Chains: 14
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Groel
UniProt: P0A6F5
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N	Groel	protein	524	50% helix, 18% strand	P0A6F5

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	990	0.81	0.83	99	empty
2	992	0.81	0.83	104	empty
3	977	0.81	0.83	104	empty
4	1014	0.81	0.82	101	empty
5	1023	0.81	0.82	104	empty

Interfaces

23 interfaces between chains.

A–G · 1790 Å² buried · 15 hydrogen bonds · protein-protein
D–E · 1786 Å² buried · 18 hydrogen bonds · protein-protein
B–C · 1751 Å² buried · 15 hydrogen bonds · protein-protein
F–G · 1733 Å² buried · 12 hydrogen bonds · protein-protein
J–K · 1728 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

2EU1 · Crystal structure of the chaperonin GroEL-E461K · the same entry in another collection · chain K against K, TM-score 1.00

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 P0A6F5
Elsewhere: RCSB PDB 2EU1 · PDBe 2EU1 · UniProt P0A6F5

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