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ATP-driven lipid-linked oligosaccharide flippase pglk in apo-inward facing state (2)

Analyse ATP-driven lipid-linked oligosaccharide flippase pglk in apo-inward facing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C76
Type: protein
Length: 2,256 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Wlab protein
UniProt: O86150
Pockets: 20 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Wlab protein	protein	564	58% helix, 4% strand	O86150

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1149	0.84	0.84	96	empty
2	1134	0.83	0.83	106	empty
3	260	0.62	0.81	30	empty
4	259	0.61	0.80	33	empty
5	216	0.60	0.81	33	empty

Interfaces

5 interfaces between chains.

B–C · 6343 Å² buried · 36 hydrogen bonds · protein-protein
A–D · 6234 Å² buried · 34 hydrogen bonds · protein-protein
A–B · 510 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 399 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 308 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5C76 · ATP-driven lipid-linked oligosaccharide flippase PglK in apo-inward facing state (2) · 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 O86150
Elsewhere: RCSB PDB 5C76 · PDBe 5C76 · UniProt O86150

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