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Crystal structure of AVRRXO1-ORF1:-ORF2 complex, native.

Analyse Crystal structure of AVRRXO1-ORF1:-ORF2 complex, native. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Z8V
Type: protein
Length: 429 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AVRRXO1-ORF1; AVRRXO1-ORF2
UniProt: Q6TKR8, Q6TKR9
Ligands: PO4
Pockets: 4 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	AVRRXO1-ORF1	protein	331	53% helix, 13% strand	Q6TKR8
B	AVRRXO1-ORF2	protein	98	66% helix, 1% strand	Q6TKR9

Ligands and binding sites

PO4 · Phosphate ion · ion · 6 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1143	0.82	0.83	116	PO4
2	303	0.64	0.80	32	PO4
3	116	0.57	0.84	30	empty
4	191	0.52	0.78	26	empty

Interfaces

1 interface between chains.

A–B · 1721 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

4Z8V · Crystal structure of AVRRXO1-ORF1:-ORF2 complex, native. · 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 Q6TKR8
Every structure of UniProt Q6TKR9
Elsewhere: RCSB PDB 4Z8V · PDBe 4Z8V · UniProt Q6TKR8 · UniProt Q6TKR9

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