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Crystal structure of pex from synechococcus sp. (strain pcc 7942) (anacystis nidulans R2)

Analyse Crystal structure of pex from synechococcus sp. (strain pcc 7942) (anacystis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZFW
Type: protein
Length: 448 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pex
UniProt: O66226
Ligands: SO4
Pockets: 5 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E	Pex	protein	112	48% helix, 13% strand	O66226

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A, B, D, E

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	495	0.69	0.79	41	SO4
2	313	0.62	0.79	27	SO4
3	154	0.55	0.81	20	SO4
4	241	0.49	0.74	27	empty
5	242	0.47	0.73	30	empty

Interfaces

4 interfaces between chains.

A–B · 1114 Å² buried · 1 hydrogen bond · protein-protein
D–E · 1048 Å² buried · 0 hydrogen bonds · protein-protein
B–D · 454 Å² buried · 1 hydrogen bond · protein-protein
A–E · 391 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2ZFW · Crystal structure of Pex from Synechococcus sp. (strain PCC 7942) (Anacystis nidulans R2) · the same entry in another collection · chain E against E, TM-score 1.00

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Every structure of UniProt O66226
Elsewhere: RCSB PDB 2ZFW · PDBe 2ZFW · UniProt O66226

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