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Crystal structure of the apo form of human RBBP7

Analyse Crystal structure of the apo form of human RBBP7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7M3X
Type: protein
Length: 378 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-binding protein RBBP7
UniProt: Q16576
Ligands: UNX
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-binding protein RBBP7	protein	378	10% helix, 46% strand	Q16576

Ligands and binding sites

UNX · Unknown atom or ion · ion · 2 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	478	0.76	0.84	35	UNX
2	106	0.51	0.82	13	empty
3	212	0.48	0.75	33	empty
4	113	0.46	0.78	17	empty

Compared structures

7M3X · Crystal Structure of the Apo Form of Human RBBP7 · the same entry in another collection · chain A against A, TM-score 1.00
Q16576 · AlphaFold monomer V2.0 prediction for histone-binding protein RBBP7 (Q16576) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q16576
Elsewhere: RCSB PDB 7M3X · PDBe 7M3X · UniProt Q16576

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