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Crystal structure of the human DMC1 protein

Analyse Crystal structure of the human DMC1 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V5W
Type: protein
Length: 478 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Meiotic recombination protein DMC1/LIM15 homolog
UniProt: Q14565
Pockets: 6 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Meiotic recombination protein DMC1/LIM15 homolog	protein	239	38% helix, 26% strand	Q14565

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	363	0.67	0.81	40	empty
2	112	0.46	0.79	21	empty
3	170	0.45	0.75	17	empty
4	137	0.43	0.76	18	empty
5	73	0.36	0.76	13	empty

Interfaces

1 interface between chains.

A–B · 1369 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

1V5W · Crystal structure of the human Dmc1 protein · the same entry in another collection · chain A against A, TM-score 1.00
Q14565 · AlphaFold monomer V2.0 prediction for meiotic recombination protein DMC1/LIM15 homolog… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q14565
Elsewhere: RCSB PDB 1V5W · PDBe 1V5W · UniProt Q14565

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