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Crystal structure of mccf homolog from listeria monocytogenes egd-E

Analyse Crystal structure of mccf homolog from listeria monocytogenes egd-E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4H1H
Type: protein
Length: 652 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LMO1638 protein
UniProt: Q8Y6P6
Ligands: SO4
Pockets: 4 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LMO1638 protein	protein	327	32% helix, 22% strand	Q8Y6P6
B	LMO1638 protein	protein	325	30% helix, 22% strand	Q8Y6P6

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B

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	968	0.84	0.85	96	SO4
2	162	0.48	0.77	21	empty
3	104	0.46	0.79	23	empty
4	141	0.46	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 1647 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 26 modified (engineered).

Compared structures

4H1H · Crystal structure of MccF homolog from Listeria monocytogenes EGD-e · 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 Q8Y6P6
Elsewhere: RCSB PDB 4H1H · PDBe 4H1H · UniProt Q8Y6P6

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