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Rmlc (dtdp-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from pseudomonas aeruginosa, apo structure

Analyse Rmlc (dtdp-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RTV
Type: protein
Length: 184 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dtdp-4-dehydrorhamnose 3,5-epimerase
EC: 5.1.3.13
UniProt: Q9HU21
Ligands: SRT
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dtdp-4-dehydrorhamnose 3,5-epimerase (EC 5.1.3.13)	protein	184	8% helix, 44% strand	Q9HU21

Ligands and binding sites

SRT · S,R meso-tartaric acid · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.46	0.83	21	SRT

Compared structures

1RTV · RmlC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from Pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00
Q9HU21 · AlphaFold monomer V2.0 prediction for dtdp-4-dehydrorhamnose 3,5-epimerase (Q9HU21) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9HU21
Elsewhere: RCSB PDB 1RTV · PDBe 1RTV · UniProt Q9HU21

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