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Crystal structure of skp

Analyse Crystal structure of skp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1U2M
Type: protein
Length: 345 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-like protein hlp-1
UniProt: P0AEU7
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 3 distinct chains · 69% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-like protein hlp-1	protein	86	55% helix, 15% strand	P0AEU7
B	Histone-like protein hlp-1	protein	116	72% helix, 12% strand	P0AEU7
C	Histone-like protein hlp-1	protein	143	76% helix, 9% strand	P0AEU7

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.33	0.77	14	empty

Interfaces

3 interfaces between chains.

A–B · 544 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 510 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 479 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

1U2M · Crystal Structure of Skp · the same entry in another collection · chain A against A, TM-score 1.00
P0AEU7 · AlphaFold monomer V2.0 prediction for chaperone protein skp (P0AEU7) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P0AEU7
Elsewhere: RCSB PDB 1U2M · PDBe 1U2M · UniProt P0AEU7

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