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Crystal structure of RRU_A2000 from rhodospirillum rubrum: a cupin-2 domain.

Analyse Crystal structure of RRU_A2000 from rhodospirillum rubrum: a cupin-2 domain. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3JZV
Type: protein
Length: 148 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein RRU_A2000
UniProt: Q2RSU5
Ligands: MN
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein RRU_A2000	protein	148	10% helix, 42% strand	Q2RSU5

Ligands and binding sites

MN · Manganese (II) ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	163	0.59	0.82	22	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

3JZV · Crystal structure of Rru_A2000 from Rhodospirillum rubrum: A cupin-2 domain. · the same entry in another collection · chain A against A, TM-score 1.00
Q2RSU5 · AlphaFold monomer V2.0 prediction for 1-methylthio-D-xylulose 5-phosphate… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q2RSU5
Elsewhere: RCSB PDB 3JZV · PDBe 3JZV · UniProt Q2RSU5

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