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F6 fused 4-ot wild type asymmetric trimer

Analyse F6 fused 4-ot wild type asymmetric trimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VVN
Type: protein
Length: 369 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-oxalocrotonate tautomerase
EC: 5.3.2.-
UniProt: A0A157ZJF6
Pockets: 5 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, C	4-oxalocrotonate tautomerase (EC 5.3.2.-)	protein	123	41% helix, 31% strand	A0A157ZJF6

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains B, C, A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	141	0.48	0.78	22	empty
2	71	0.41	0.79	16	GOL
3	87	0.39	0.77	18	empty
4	67	0.39	0.79	16	GOL
5	80	0.35	0.76	21	empty

Interfaces

3 interfaces between chains.

B–A · 1343 Å² buried · 23 hydrogen bonds · protein-protein
A–C · 1325 Å² buried · 23 hydrogen bonds · protein-protein
B–C · 1320 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6VVN · F6 fused 4-OT wild type asymmetric trimer · the same entry in another collection · chain B against B, 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 A0A157ZJF6
Elsewhere: RCSB PDB 6VVN · PDBe 6VVN · UniProt A0A157ZJF6

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