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Crystal structure of an ASPARTATE/GLUTAMATE racemase in complex with D-aspartate

Analyse Crystal structure of an ASPARTATE/GLUTAMATE racemase in complex with D-aspartate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HRA
Type: protein
Length: 465 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ASPARTATE/GLUTAMATE racemase
UniProt: A0A0F6FBL7
Ligands: DAS
Pockets: 2 · best druggability 0.28

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ASPARTATE/GLUTAMATE racemase	protein	233	59% helix, 12% strand	A0A0F6FBL7
B	ASPARTATE/GLUTAMATE racemase	protein	232	59% helix, 13% strand	A0A0F6FBL7

Ligands and binding sites

DAS · D-aspartic acid · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.28	0.74	15	empty
2	55	0.27	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 1571 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

5HRA · Crystal structure of an aspartate/glutamate racemase in complex with D-aspartate · 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 A0A0F6FBL7
Elsewhere: RCSB PDB 5HRA · PDBe 5HRA · UniProt A0A0F6FBL7

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