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Malyl-CoA lyase from methylobacterium extorquens

Analyse Malyl-CoA lyase from methylobacterium extorquens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UGR
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Malyl-CoA LYASE/BETA-methylmalyl-CoA lyase
EC: 4.1.3.24
UniProt: C5B113
Ligands: MG, CL
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Malyl-CoA LYASE/BETA-methylmalyl-CoA lyase (EC 4.1.3.24)	protein	323	46% helix, 16% strand	C5B113

Ligands and binding sites

MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · chains A
1PE · Pentaethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	272	0.61	0.79	41	empty
2	97	0.43	0.78	18	CL
3	79	0.34	0.75	16	empty
4	69	0.34	0.75	12	empty

Compared structures

5UGR · Malyl-CoA lyase from Methylobacterium extorquens · 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 C5B113
Elsewhere: RCSB PDB 5UGR · PDBe 5UGR · UniProt C5B113

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