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Structure of a minimal complex between P44 and P34 from chaetomium thermophilum

Analyse Structure of a minimal complex between P44 and P34 from chaetomium thermophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NUS
Type: protein
Length: 285 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P34; P44
UniProt: G0RXV8, G0RZE6
Ligands: ZN
Pockets: 3 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P34	protein	211	50% helix, 19% strand	G0RXV8
B	P44	protein	74	28% helix, 12% strand	G0RZE6

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	170	0.46	0.76	25	empty
2	124	0.44	0.77	25	empty
3	56	0.30	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 1063 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5NUS · Structure of a minimal complex between p44 and p34 from Chaetomium thermophilum · 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 G0RXV8
Every structure of UniProt G0RZE6
Elsewhere: RCSB PDB 5NUS · PDBe 5NUS · UniProt G0RXV8 · UniProt G0RZE6

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