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C-terminal domain of kipi from bacillus subtilis

Analyse C-terminal domain of kipi from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZP2
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinase a inhibitor
UniProt: P60495
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinase a inhibitor	protein	121	15% helix, 31% strand	P60495
B	Kinase a inhibitor	protein	123	13% helix, 32% strand	P60495

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	238	0.51	0.75	23	empty

Interfaces

1 interface between chains.

A–B · 15 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2ZP2 · C-terminal domain of KipI from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
P60495 · AlphaFold monomer V2.0 prediction for 5-oxoprolinase subunit B (P60495) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P60495
Elsewhere: RCSB PDB 2ZP2 · PDBe 2ZP2 · UniProt P60495

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