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X-ray crystal structure of protein ATU5096 from agrobacterium tumefaciens. northeast structural genomics consortium target ATR63.

Analyse X-ray crystal structure of protein ATU5096 from agrobacterium tumefaciens.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AEG
Type: protein
Length: 729 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein AGR_PAT_140
UniProt: Q8UKK6
Pockets: 7 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Hypothetical protein AGR_PAT_140	protein	243	23% helix, 32% strand	Q8UKK6

Pockets

7 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	276	0.63	0.81	32	empty
2	102	0.41	0.76	17	empty
3	103	0.40	0.76	18	empty
4	97	0.38	0.75	17	empty
5	82	0.34	0.75	24	empty

Interfaces

2 interfaces between chains.

B–C · 305 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 53 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 modified (engineered).

Compared structures

2AEG · X-Ray Crystal Structure of Protein Atu5096 from Agrobacterium tumefaciens. Northeast… · 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 Q8UKK6
Elsewhere: RCSB PDB 2AEG · PDBe 2AEG · UniProt Q8UKK6

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