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Crystal structure of DNA damage-binding protein 1(DDB1)

Analyse Crystal structure of DNA damage-binding protein 1(DDB1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3E0C
Type: protein
Length: 1,011 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA damage-binding protein 1
UniProt: Q16531
Pockets: 10 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA damage-binding protein 1	protein	1011	6% helix, 53% strand	Q16531

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	987	0.79	0.81	89	empty
2	1084	0.76	0.78	79	empty
3	763	0.71	0.77	59	empty
4	644	0.70	0.78	43	empty
5	63	0.58	0.89	19	empty

Compared structures

3E0C · Crystal Structure of DNA Damage-Binding protein 1(DDB1) · the same entry in another collection · chain A against A, TM-score 1.00
Q16531 · AlphaFold monomer V2.0 prediction for DNA damage-binding protein 1 (Q16531) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 Q16531
Elsewhere: RCSB PDB 3E0C · PDBe 3E0C · UniProt Q16531

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