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Crystal structure of threonine aldolase from Mycobacterium vanbaalenii

Analyse Crystal structure of threonine aldolase from Mycobacterium vanbaalenii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7W0I
Type: protein
Length: 1,336 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.75
Source: Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC…
Molecule: L-threonine aldolase
EC: 4.1.2.48
UniProt: A1T4B4
Pockets: 9 · best druggability 0.84

Structure

x-ray diffraction · resolution 1.75 · 1 distinct chain · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	L-threonine aldolase (EC 4.1.2.48)	protein	334	45% helix, 16% strand	A1T4B4

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1075	0.84	0.85	150	empty
2	1199	0.83	0.84	160	empty
3	221	0.81	0.95	41	empty
4	60	0.36	0.79	14	empty
5	82	0.36	0.76	16	empty

Interfaces

6 interfaces between chains.

C–D · 2089 Å² buried · 40 hydrogen bonds · protein-protein
A–B · 2077 Å² buried · 40 hydrogen bonds · protein-protein
B–D · 1160 Å² buried · 17 hydrogen bonds · protein-protein
A–C · 1156 Å² buried · 20 hydrogen bonds · protein-protein
A–D · 840 Å² buried · 6 hydrogen bonds · protein-protein

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A1T4B4
Elsewhere: RCSB PDB 7W0I · PDBe 7W0I · UniProt A1T4B4

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