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Structure of parf-ADP, crystal form 1

Analyse Structure of parf-ADP, crystal form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DZZ
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Plasmid partitioning protein parf
UniProt: B0ZE06
Ligands: ADP, MG
Pockets: 4 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Plasmid partitioning protein parf	protein	206	44% helix, 18% strand	B0ZE06

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	128	0.52	0.81	26	empty
2	129	0.46	0.78	27	ADP, MG
3	119	0.43	0.77	27	ADP, MG
4	58	0.28	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 693 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4DZZ · Structure of ParF-ADP, crystal form 1 · 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 B0ZE06
Elsewhere: RCSB PDB 4DZZ · PDBe 4DZZ · UniProt B0ZE06

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