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Crystal structure of TT0168 from thermus thermophilus HB8

Analyse Crystal structure of TT0168 from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ULT
Type: protein
Length: 1,047 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Long chain fatty acid-CoA ligase
EC: 6.2.1.3
UniProt: Q6L8F0
Pockets: 10 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Long chain fatty acid-CoA ligase (EC 6.2.1.3)	protein	533	31% helix, 24% strand	Q6L8F0
B	Long chain fatty acid-CoA ligase (EC 6.2.1.3)	protein	514	32% helix, 23% strand	Q6L8F0

Ligands and binding sites

CIT · Citric acid · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	822	0.68	0.75	67	empty
2	683	0.67	0.76	67	CIT
3	208	0.62	0.82	35	empty
4	185	0.60	0.82	30	empty
5	243	0.51	0.75	38	empty

Interfaces

1 interface between chains.

A–B · 3003 Å² buried · 45 hydrogen bonds · protein-protein

Compared structures

1ULT · Crystal structure of tt0168 from Thermus thermophilus HB8 · the same entry in another collection · chain B against B, 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 Q6L8F0
Elsewhere: RCSB PDB 1ULT · PDBe 1ULT · UniProt Q6L8F0

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