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A structural study of the ca dinucleotide step in the integrase processing site of moloney murine leukemia virus

Analyse A structural study of the ca dinucleotide step in the integrase processing site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FVQ
Type: protein + DNA
Length: 271 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5'- D(*CP*TP*TP*TP*CP*AP*TP*TP*AP*AP*TP*GP*AP*AP*AP*G)-3'; Reverse transcriptase
EC: 2.7.7.49
UniProt: P03355
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	5'- D(CPTPTPTPCPAPTPTPAPAPTPGPAPAPAPG)-3'	dna	16	—	—
A	Reverse transcriptase (EC 2.7.7.49)	protein	255	31% helix, 24% strand	P03355

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	147	0.44	0.75	28	empty

Interfaces

1 interface between chains.

B–A · 220 Å² buried · 5 hydrogen bonds · protein-nucleic

Compared structures

2FVQ · A Structural Study of the CA Dinucleotide Step in the Integrase Processing Site of… · the same entry in another collection · chain B against B, 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 P03355
Elsewhere: RCSB PDB 2FVQ · PDBe 2FVQ · UniProt P03355

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