MolNFT v1 · #56816 · protein

Msreca Q196A ADP form IV

2ZRI · Protein reca: “Msreca Q196A ADP form IV”. X-ray diffraction, 1 ligand (ADP), 4 pockets (best druggability 0.46). MolNFT v1 #56816 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2ZRI
Type: protein
Length: 317 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein reca
EC: 3.4.99.37
UniProt: Q59560
Ligands: ADP
Pockets: 4 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein reca (EC 3.4.99.37)	protein	317	39% helix, 21% strand	Q59560

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

4 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	199	0.46	0.74	30	ADP
2	100	0.36	0.74	23	empty
3	68	0.34	0.76	16	empty
4	60	0.28	0.74	13	empty

Compared structures

2ZRI · MsRecA Q196A ADP 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 0.85

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 2ZRI · PDBe 2ZRI · UniProt Q59560

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