MolNFT v1 · #106440 · protein

Transaldolase B E96Q from E.COLI

4RZ5: “Transaldolase B E96Q from E.COLI”. X-ray diffraction, 1 ligand (SO4), 6 pockets (best druggability 0.82). MolNFT v1 #106440 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4RZ5
Type: protein
Length: 632 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transaldolase B
EC: 2.2.1.2
UniProt: P0A870
Ligands: SO4
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transaldolase B (EC 2.2.1.2)	protein	316	56% helix, 13% strand	P0A870

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B

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

Pockets

6 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	173	0.82	0.97	27	empty
2	118	0.45	0.78	23	SO4
3	105	0.42	0.77	21	SO4
4	52	0.30	0.75	12	empty
5	62	0.29	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 814 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

4RZ5 · Transaldolase B E96Q from E.coli · the same entry in another collection · chain A against A, TM-score 1.00
P0A870 · AlphaFold monomer V2.0 prediction for transaldolase B (P0A870) · a predicted model of the same protein · 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 P0A870
Elsewhere: RCSB PDB 4RZ5 · PDBe 4RZ5 · UniProt P0A870

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