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Crystal structure of het-C2: a fungal glycolipid transfer protein (gltp)

Analyse Crystal structure of het-C2: a fungal glycolipid transfer protein (gltp) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KV0
Type: protein
Length: 194 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Het-C2
UniProt: Q01494
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Het-C2	protein	194	75% helix, 3% strand	Q01494

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.37	0.76	16	empty

Modifications

Observed in the structure: 17 modified (methylation).

Compared structures

3KV0 · Crystal structure of HET-C2: A FUNGAL GLYCOLIPID TRANSFER PROTEIN (GLTP) · 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 Q01494
Elsewhere: RCSB PDB 3KV0 · PDBe 3KV0 · UniProt Q01494

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