MolNFT v1 · #98525 · protein

Meab, a bacterial homolog of mmaa, bound to GDP and crystallized in the presence of GDP and [ALF4]-

4LC1 · Methylmalonyl-CoA mutase accessory protein: “Meab, a bacterial homolog of mmaa, bound to GDP and crystallized in the presence of GDP and [ALF4]-”. X-ray diffraction, 1 ligand (GDP), 8 pockets (best druggability 0.71). MolNFT v1…

PDB: 4LC1
Type: protein
Length: 623 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methylmalonyl-CoA mutase accessory protein
UniProt: C5AP93
Ligands: GDP
Pockets: 8 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methylmalonyl-CoA mutase accessory protein	protein	315	54% helix, 12% strand	C5AP93
B	Methylmalonyl-CoA mutase accessory protein	protein	308	55% helix, 12% strand	C5AP93

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	729	0.71	0.77	71	empty
2	263	0.70	0.85	33	empty
3	195	0.68	0.86	33	empty
4	342	0.66	0.81	46	empty
5	111	0.44	0.78	22	empty

Interfaces

1 interface between chains.

A–B · 2638 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

4LC1 · MeaB, A Bacterial Homolog of MMAA, Bound to GDP and crystallized in the presence of GDP… · 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 C5AP93
Elsewhere: RCSB PDB 4LC1 · PDBe 4LC1 · UniProt C5AP93

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