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Crystal structure of chlamydomonas reinhardtii thioredoxin F2

Analyse Crystal structure of chlamydomonas reinhardtii thioredoxin F2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6I1C
Type: protein
Length: 318 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin F2
UniProt: A0A2K3DSC9
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 3 distinct chains · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin F2	protein	108	38% helix, 26% strand	A0A2K3DSC9
B	Thioredoxin F2	protein	103	37% helix, 23% strand	A0A2K3DSC9
C	Thioredoxin F2	protein	107	32% helix, 24% strand	A0A2K3DSC9

Pockets

3 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	66	0.45	0.83	14	empty
2	186	0.43	0.73	24	empty
3	82	0.41	0.79	16	empty

Interfaces

2 interfaces between chains.

A–B · 558 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 451 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6I1C · Crystal structure of Chlamydomonas reinhardtii thioredoxin f2 · 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 A0A2K3DSC9
Elsewhere: RCSB PDB 6I1C · PDBe 6I1C · UniProt A0A2K3DSC9

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