Research workbench

MsRecA Q196A form IV

Analyse MsRecA Q196A form IV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZRH
Type: protein
Length: 319 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.2
Source: Mycobacterium smegmatis str. MC2 155
Molecule: Protein recA
EC: 3.4.99.37
UniProt: Q59560
Ligands: PO4
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · resolution 3.2 · 1 distinct chain · 41% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein recA (EC 3.4.99.37)	protein	319	41% helix, 24% strand	Q59560

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	187	0.49	0.76	30	PO4
2	137	0.44	0.76	22	empty
3	88	0.32	0.73	23	empty
4	50	0.25	0.73	14	empty
5	50	0.25	0.73	19	empty

Compared structures

2ZRH · Msreca Q196A form IV · the same entry in another collection · chain A against A, TM-score 1.00
Q59560 · AlphaFold monomer V2.0 prediction for protein reca (Q59560) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 Q59560
Elsewhere: RCSB PDB 2ZRH · PDBe 2ZRH · UniProt Q59560

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