MolNFT v1 · #97149 · protein

Co-crystallization with conformation-specific designed ankyrin repeat proteins explains the conformational flexibility of BCL-W

4K5A · BCL-2-like protein 2: “Co-crystallization with conformation-specific designed ankyrin repeat proteins explains the conformational…”. X-ray diffraction, 1 pocket (best druggability 0.70). MolNFT v1 #97149 on GenesisL1: 3D structure…

PDB: 4K5A
Type: protein
Length: 325 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BCL-2-like protein 2; Designed ankyrin repeat protein 013_D12
UniProt: Q1RMX3
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BCL-2-like protein 2	protein	164	63% helix, 0% strand	Q1RMX3
B	Designed ankyrin repeat protein 013_D12	protein	161	58% helix, 0% strand	—

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	137	0.70	0.90	22	empty

Interfaces

1 interface between chains.

A–B · 912 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4K5A · Co-crystallization with conformation-specific designed ankyrin repeat proteins explains… · the same entry in another collection · chain A against A, TM-score 1.00
Q1RMX3 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 2 (Q1RMX3) · a predicted model of the same protein · chain A against A, TM-score 0.86

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 Q1RMX3
Elsewhere: RCSB PDB 4K5A · PDBe 4K5A · UniProt Q1RMX3

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