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Crystal structure of apo adenylosuccinate lyase from mycobacterium smegmatis

Analyse Crystal structure of apo adenylosuccinate lyase from mycobacterium smegmatis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NLE
Type: protein
Length: 915 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylosuccinate lyase
EC: 4.3.2.2
UniProt: A0R4I6
Pockets: 13 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenylosuccinate lyase (EC 4.3.2.2)	protein	464	67% helix, 4% strand	A0R4I6
B	Adenylosuccinate lyase (EC 4.3.2.2)	protein	451	69% helix, 4% strand	A0R4I6

Pockets

13 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	70	0.75	0.99	22	empty
2	71	0.74	0.98	21	empty
3	250	0.56	0.77	35	empty
4	266	0.54	0.76	35	empty
5	75	0.52	0.85	19	empty

Interfaces

1 interface between chains.

A–B · 3100 Å² buried · 75 hydrogen bonds · protein-protein

Compared structures

4NLE · Crystal structure of apo Adenylosuccinate Lyase from Mycobacterium smegmatis · 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 A0R4I6
Elsewhere: RCSB PDB 4NLE · PDBe 4NLE · UniProt A0R4I6

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