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The crystal structure of human glia maturation factor, gamma (gmfg)

Analyse The crystal structure of human glia maturation factor, gamma (gmfg) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3L50
Type: protein
Length: 272 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glia maturation factor gamma
UniProt: O60234
Ligands: CL
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glia maturation factor gamma	protein	136	34% helix, 27% strand	O60234

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains B

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

Pockets

2 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	183	0.71	0.88	27	empty
2	58	0.30	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 649 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3L50 · The crystal structure of human Glia Maturation Factor, Gamma (GMFG) · the same entry in another collection · chain A against A, TM-score 1.00
O60234 · AlphaFold monomer V2.0 prediction for glia maturation factor gamma (O60234) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 O60234
Elsewhere: RCSB PDB 3L50 · PDBe 3L50 · UniProt O60234

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