MolNFT v1 · #121301 · protein

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

5HRC: “Crystal structure of an ASPARTATE/GLUTAMATE racemase in complex with L-aspartate”. X-ray diffraction, 1 ligand (ASP), 1 pocket (best druggability 0.30). MolNFT v1 #121301 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5HRC
Type: protein
Length: 463 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ASPARTATE/GLUTAMATE racemase
UniProt: A0A0F6FBL7
Ligands: ASP
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ASPARTATE/GLUTAMATE racemase	protein	232	58% helix, 13% strand	A0A0F6FBL7
B	ASPARTATE/GLUTAMATE racemase	protein	231	58% helix, 12% strand	A0A0F6FBL7

Ligands and binding sites

ASP · Aspartic acid · ligand · 2 copies · chains A, B
NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · chains A, B

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	54	0.30	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 1566 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

5HRC · Crystal structure of an aspartate/glutamate racemase in complex with L-aspartate · the same entry in another collection · chain B against B, 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 5HRC · PDBe 5HRC · UniProt A0A0F6FBL7

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