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Crystal structure of apo transketolase from chlamydomonas reinhardtii

Analyse Crystal structure of apo transketolase from chlamydomonas reinhardtii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ND6
Type: protein
Length: 1,339 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transketolase
EC: 2.2.1.1
UniProt: A8IAN1
Pockets: 9 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transketolase (EC 2.2.1.1)	protein	669	45% helix, 12% strand	A8IAN1
B	Transketolase (EC 2.2.1.1)	protein	670	44% helix, 12% strand	A8IAN1

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains A

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

Pockets

9 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	313	0.75	0.87	49	empty
2	790	0.72	0.77	78	empty
3	259	0.70	0.85	38	empty
4	90	0.54	0.84	24	empty
5	142	0.53	0.81	34	empty

Interfaces

1 interface between chains.

A–B · 4189 Å² buried · 63 hydrogen bonds · protein-protein

Compared structures

5ND6 · Crystal structure of apo transketolase from Chlamydomonas reinhardtii · 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 A8IAN1
Elsewhere: RCSB PDB 5ND6 · PDBe 5ND6 · UniProt A8IAN1

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