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Crystal structure of the rous associated virus integrase catalytic domain in mes buffer pH 6.0

Analyse Crystal structure of the rous associated virus integrase catalytic domain in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3O4N
Type: protein
Length: 270 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Integrase
UniProt: Q4ZJZ6
Ligands: ZN
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Integrase	protein	133	48% helix, 20% strand	Q4ZJZ6
B	Integrase	protein	137	49% helix, 20% strand	Q4ZJZ6

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A, B
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	246	0.73	0.88	31	MES
2	285	0.70	0.84	33	empty
3	125	0.43	0.76	17	ZN

Interfaces

1 interface between chains.

A–B · 804 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3O4N · Crystal structure of the Rous Associated Virus Integrase catalytic domain in MES buffer… · 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 Q4ZJZ6
Elsewhere: RCSB PDB 3O4N · PDBe 3O4N · UniProt Q4ZJZ6

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