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Crystal structure of the uncharacterized maf protein ycef from E. COLI, mutant D69A

Analyse Crystal structure of the uncharacterized maf protein ycef from E. COLI, mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LU1
Type: protein
Length: 369 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maf-like protein ycef
UniProt: C9QYM5
Ligands: UNX
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Maf-like protein ycef	protein	191	34% helix, 27% strand	C9QYM5
B	Maf-like protein ycef	protein	178	35% helix, 28% strand	C9QYM5

Ligands and binding sites

UNX · Unknown atom or ion · ion · 2 copies · chains A, B

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

Pockets

3 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	177	0.60	0.82	27	empty
2	345	0.59	0.76	33	empty
3	180	0.44	0.74	27	empty

Interfaces

1 interface between chains.

A–B · 1431 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4LU1 · Crystal structure of the uncharacterized Maf protein YceF from E. coli, mutant D69A · 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 C9QYM5
Elsewhere: RCSB PDB 4LU1 · PDBe 4LU1 · UniProt C9QYM5

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