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Human RAD52 protein, N-terminal domain

Analyse Human RAD52 protein, N-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H2I
Type: protein
Length: 4,092 residues
Chains: 22
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA repair protein RAD52 homolog
UniProt: P43351
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V	DNA repair protein RAD52 homolog	protein	186	37% helix, 28% strand	P43351

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1199	0.80	0.81	87	empty
2	853	0.78	0.81	103	empty
3	867	0.78	0.81	101	empty
4	577	0.74	0.81	73	empty
5	578	0.73	0.81	71	empty

Interfaces

49 interfaces between chains.

Q–R · 2677 Å² buried · 39 hydrogen bonds · protein-protein
O–P · 2671 Å² buried · 39 hydrogen bonds · protein-protein
B–C · 2667 Å² buried · 41 hydrogen bonds · protein-protein
R–S · 2667 Å² buried · 38 hydrogen bonds · protein-protein
C–D · 2663 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

1H2I · Human Rad52 protein, N-terminal domain · the same entry in another collection · chain V against V, TM-score 1.00

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 P43351
Elsewhere: RCSB PDB 1H2I · PDBe 1H2I · UniProt P43351

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