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Pyruvate kinase from E. COLI in the T-state

Analyse Pyruvate kinase from E. COLI in the T-state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PKY
Type: protein
Length: 1,825 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyruvate kinase
EC: 2.7.1.40
UniProt: P14178
Pockets: 20 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	Pyruvate kinase (EC 2.7.1.40)	protein	464	39% helix, 23% strand	P14178
C	Pyruvate kinase (EC 2.7.1.40)	protein	433	40% helix, 20% strand	P14178

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	907	0.75	0.78	104	empty
2	97	0.73	0.95	27	empty
3	182	0.70	0.88	38	empty
4	682	0.69	0.77	81	empty
5	434	0.67	0.79	59	empty

Interfaces

4 interfaces between chains.

A–C · 1114 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 1086 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 933 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 904 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

1PKY · Pyruvate kinase from E. COLI in the T-state · the same entry in another collection · chain D against D, 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 P14178
Elsewhere: RCSB PDB 1PKY · PDBe 1PKY · UniProt P14178

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