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Crystal structure of a putative thioesterase (SYN_01977) from syntrophus aciditrophicus sb at 2.50 a resolution

Analyse Crystal structure of a putative thioesterase (SYN_01977) from syntrophus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HDU
Type: protein
Length: 451 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative thioesterase
UniProt: Q2LUI2
Pockets: 2 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 38% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative thioesterase	protein	152	38% helix, 38% strand	Q2LUI2
B	Putative thioesterase	protein	148	36% helix, 39% strand	Q2LUI2
C	Putative thioesterase	protein	151	38% helix, 38% strand	Q2LUI2

Pockets

2 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	218	0.82	0.95	35	empty
2	230	0.53	0.77	29	empty

Interfaces

2 interfaces between chains.

A–B · 1714 Å² buried · 31 hydrogen bonds · protein-protein
B–C · 344 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 27 modified (engineered).

Compared structures

3HDU · Crystal structure of a putative thioesterase (SYN_01977) from syntrophus aciditrophicus… · 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 Q2LUI2
Elsewhere: RCSB PDB 3HDU · PDBe 3HDU · UniProt Q2LUI2

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