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Crystal structure of the urease accessory protein uref from klebsiella pneumoniae

Analyse Crystal structure of the urease accessory protein uref from klebsiella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JC4
Type: protein
Length: 800 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Urease accessory protein uref
UniProt: A0A2X3G2L5
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Urease accessory protein uref	protein	200	78% helix, 0% strand	A0A2X3G2L5

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	125	0.72	0.92	28	empty
2	138	0.70	0.90	27	empty
3	133	0.69	0.89	26	empty
4	125	0.66	0.88	25	empty
5	489	0.60	0.74	41	empty

Interfaces

4 interfaces between chains.

A–D · 1814 Å² buried · 27 hydrogen bonds · protein-protein
B–C · 1791 Å² buried · 33 hydrogen bonds · protein-protein
A–C · 179 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 41 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6JC4 · Crystal structure of the urease accessory protein UreF from Klebsiella pneumoniae · 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 A0A2X3G2L5
Elsewhere: RCSB PDB 6JC4 · PDBe 6JC4 · UniProt A0A2X3G2L5

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