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Crystal structure of SEC14-like protein 4 (SEC14L4)

Analyse Crystal structure of SEC14-like protein 4 (SEC14L4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TLG
Type: protein
Length: 784 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SEC14-like protein 4
UniProt: Q9UDX3
Ligands: 11A
Pockets: 13 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SEC14-like protein 4	protein	396	37% helix, 23% strand	Q9UDX3
B	SEC14-like protein 4	protein	388	40% helix, 24% strand	Q9UDX3

Ligands and binding sites

11A · Undecanoic acid · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 26 copies · chains A, B

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

Pockets

13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	196	0.83	0.96	26	11A
2	178	0.83	0.97	26	11A
3	66	0.71	0.96	23	EDO
4	124	0.59	0.85	24	EDO
5	267	0.53	0.75	27	EDO

Interfaces

1 interface between chains.

A–B · 145 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4TLG · Crystal structure of SEC14-like protein 4 (SEC14L4) · the same entry in another collection · chain A against A, TM-score 1.00
Q9UDX3 · AlphaFold monomer V2.0 prediction for SEC14-like protein 4 (Q9UDX3) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 Q9UDX3
Elsewhere: RCSB PDB 4TLG · PDBe 4TLG · UniProt Q9UDX3

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