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Thne from S.CLAVULIGERUS

Analyse Thne from S.CLAVULIGERUS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5O34
Type: protein
Length: 608 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-CoA hydratase carb homologue
UniProt: Q83XP9
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 55% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-CoA hydratase carb homologue	protein	209	56% helix, 17% strand	Q83XP9
B	Enoyl-CoA hydratase carb homologue	protein	203	56% helix, 17% strand	Q83XP9
C	Enoyl-CoA hydratase carb homologue	protein	196	54% helix, 19% strand	Q83XP9

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1069	0.78	0.80	78	empty
2	187	0.53	0.78	24	empty
3	124	0.47	0.78	16	empty
4	95	0.39	0.76	15	empty

Interfaces

3 interfaces between chains.

B–C · 982 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 972 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 943 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

5O34 · ThnE from S.clavuligerus · the same entry in another collection · chain A against A, 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 Q83XP9
Elsewhere: RCSB PDB 5O34 · PDBe 5O34 · UniProt Q83XP9

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