MolNFT v1 · #166846 · protein

Structure of escherichia COLI ASP269ASN mutant phosphoenolpyruvate carboxykinase

6V2M · Phosphoenolpyruvate carboxykinase (ATP): “Structure of escherichia COLI ASP269ASN mutant phosphoenolpyruvate carboxykinase”. X-ray diffraction, 3 ligands (ATP, MG, CA), 3 pockets (best druggability 0.71). MolNFT v1 #166846 on…

PDB: 6V2M
Type: protein
Length: 531 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoenolpyruvate carboxykinase (ATP)
EC: 4.1.1.49
UniProt: A0A400L9R1
Ligands: ATP, MG, CA
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49)	protein	531	32% helix, 24% strand	A0A400L9R1

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
CA · Calcium ion · metal · chains A

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

Pockets

3 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	622	0.71	0.79	72	ATP, MG, CA
2	100	0.40	0.77	22	empty
3	52	0.32	0.77	13	empty

Compared structures

6V2M · Structure of Escherichia coli Asp269Asn mutant phosphoenolpyruvate carboxykinase · 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 A0A400L9R1
Elsewhere: RCSB PDB 6V2M · PDBe 6V2M · UniProt A0A400L9R1

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