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Convergent evolution of similar function in two structurally divergent enzymes

Analyse Convergent evolution of similar function in two structurally divergent enzymes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TRB
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin reductase
EC: 1.6.4.5
UniProt: P0A9P4
Ligands: FAD
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin reductase (EC 1.6.4.5)	protein	316	29% helix, 28% strand	P0A9P4

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	502	0.79	0.86	75	FAD
2	58	0.34	0.77	14	empty
3	63	0.28	0.74	21	empty
4	68	0.28	0.73	16	empty

Compared structures

1TRB · Convergent evolution of similar function in two structurally divergent enzymes · the same entry in another collection · chain A against A, TM-score 1.00
P0A9P4 · AlphaFold monomer V2.0 prediction for thioredoxin reductase (P0A9P4) · a predicted model of the same protein · chain A against A, TM-score 0.73

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 P0A9P4
Elsewhere: RCSB PDB 1TRB · PDBe 1TRB · UniProt P0A9P4

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