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Tryptophan--tRNA ligase from haemophilus influenzae.

Analyse Tryptophan--tRNA ligase from haemophilus influenzae. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DFU
Type: protein
Length: 663 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tryptophan--tRNA ligase
EC: 6.1.1.2
UniProt: P43835
Ligands: TRP
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tryptophan--tRNA ligase (EC 6.1.1.2)	protein	332	58% helix, 8% strand	P43835
B	Tryptophan--tRNA ligase (EC 6.1.1.2)	protein	331	58% helix, 8% strand	P43835

Ligands and binding sites

TRP · Tryptophan · ligand · 2 copies · chains A, B

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

Pockets

6 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	797	0.72	0.77	60	TRP
2	386	0.64	0.78	36	TRP
3	122	0.44	0.77	24	empty
4	119	0.43	0.77	23	empty
5	86	0.42	0.79	22	empty

Interfaces

1 interface between chains.

A–B · 2481 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

6DFU · Tryptophan--tRNA ligase from Haemophilus influenzae. · the same entry in another collection · chain A against A, TM-score 1.00
P43835 · AlphaFold monomer V2.0 prediction for tryptophan--tRNA ligase (P43835) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P43835
Elsewhere: RCSB PDB 6DFU · PDBe 6DFU · UniProt P43835

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