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Pepck steady-state structure with mn and GTP

Analyse Pepck steady-state structure with mn and GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7L36
Type: protein
Length: 613 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
EC: 4.1.1.32, 2.7.11.-
UniProt: P07379
Ligands: GTP, MN, CL
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (EC 4.1.1.32, 2.7.11.-)	protein	613	31% helix, 23% strand	P07379

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · chains A
MN · Manganese (II) ion · metal · 3 copies · chains A
CL · Chloride ion · ion · chains A

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

Pockets

7 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	446	0.70	0.81	54	MN, GTP
2	158	0.58	0.82	20	CL
3	86	0.46	0.81	18	empty
4	57	0.39	0.80	23	empty
5	61	0.35	0.78	18	empty

Compared structures

7L36 · PEPCK steady-state structure with Mn and GTP · 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 P07379
Elsewhere: RCSB PDB 7L36 · PDBe 7L36 · UniProt P07379

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