MolNFT v1 · #171044 · protein

Transaldolase variant T30C/D211C from T. acidophilum

6YRE: “Transaldolase variant T30C/D211C from T. acidophilum”. X-ray diffraction. MolNFT v1 #171044 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6YRE
Type: protein
Length: 1,093 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9HKI3

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	—	protein	218	—	Q9HKI3
B, E	—	protein	217	—	Q9HKI3
C	—	protein	223	—	Q9HKI3

Ligands and binding sites

GOL · Glycerol · additive · 6 copies · chains A, B, C, D, E
ACT · Acetate ion · additive · 5 copies · chains A, E, B, C

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

Compared structures

6YRE · Transaldolase variant T30C/D211C from T. acidophilum · the same entry in another collection · chain E against E, TM-score 1.00
Q9HKI3 · AlphaFold monomer V2.0 prediction for probable transaldolase (Q9HKI3) · a predicted model of the same protein · chain C 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 Q9HKI3
Elsewhere: RCSB PDB 6YRE · PDBe 6YRE · UniProt Q9HKI3

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