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The crystal structure of unliganded phosphofructokinase from escherichia COLI

Analyse The crystal structure of unliganded phosphofructokinase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PFK
Type: protein
Length: 1,208 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 6-phosphofructokinase isozyme I
EC: 2.7.1.11
Pockets: 17 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	6-phosphofructokinase isozyme I (EC 2.7.1.11)	protein	301	46% helix, 20% strand	—
D	6-phosphofructokinase isozyme I (EC 2.7.1.11)	protein	305	45% helix, 20% strand	—

Pockets

17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	178	0.56	0.80	21	empty
2	268	0.56	0.77	44	empty
3	158	0.54	0.80	18	empty
4	240	0.52	0.76	35	empty
5	244	0.52	0.76	31	empty

Interfaces

2 interfaces between chains.

C–D · 1042 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 1030 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2PFK · The crystal structure of unliganded phosphofructokinase from escherichia COLI · 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
Elsewhere: RCSB PDB 2PFK · PDBe 2PFK

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