Research workbench

Structure of hpdpra at 1.9 ångströms resolution

Analyse Structure of hpdpra at 1.9 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MLL
Type: protein
Length: 436 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA processing chain a (dpra)
UniProt: O25100
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA processing chain a (dpra)	protein	218	42% helix, 16% strand	O25100
B	DNA processing chain a (dpra)	protein	218	42% helix, 16% strand	O25100

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	576	0.67	0.77	46	empty
2	173	0.58	0.81	28	empty
3	186	0.55	0.79	26	empty
4	96	0.36	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 453 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5MLL · Structure of HpDprA at 1.9 Angstroms resolution · the same entry in another collection · chain A against A, 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 O25100
Elsewhere: RCSB PDB 5MLL · PDBe 5MLL · UniProt O25100

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.