MolNFT v1 · #117884 · protein

Crystal structure of L-ASPARTATE/GLUTAMATE-specific racemase from escherichia COLI

5ELL · ASP/GLU_RACEMASE family protein: “Crystal structure of L-ASPARTATE/GLUTAMATE-specific racemase from escherichia COLI”. X-ray diffraction, 5 pockets (best druggability 0.67). MolNFT v1 #117884 on GenesisL1: 3D structure, binding…

PDB: 5ELL
Type: protein
Length: 466 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ASP/GLU_RACEMASE family protein
EC: 5.1.1.13
UniProt: C3SWD2
Pockets: 5 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 59% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ASP/GLU_RACEMASE family protein (EC 5.1.1.13)	protein	231	60% helix, 13% strand	C3SWD2
B	ASP/GLU_RACEMASE family protein (EC 5.1.1.13)	protein	235	59% helix, 12% strand	C3SWD2

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	370	0.67	0.80	47	empty
2	415	0.65	0.78	48	empty
3	95	0.35	0.74	20	empty
4	64	0.32	0.75	12	empty
5	55	0.27	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 1388 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

5ELL · Crystal structure of L-aspartate/glutamate-specific racemase from Escherichia coli · 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 C3SWD2
Elsewhere: RCSB PDB 5ELL · PDBe 5ELL · UniProt C3SWD2

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