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D(CTTGAATGCATTCAAG) in complex with mmlv rt catalytic fragment

Analyse D(CTTGAATGCATTCAAG) in complex with mmlv rt catalytic fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FJW
Type: protein + DNA
Length: 271 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5'-D(*CP*TP*TP*GP*AP*AP*TP*G)-3'; 5'-D(P*CP*AP*TP*TP*CP*AP*AP*G)-3'; Reverse transcriptase
EC: 2.7.7.49
UniProt: P03355
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 3 distinct chains · 30% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	5'-D(CPTPTPGPAPAPTPG)-3'	dna	8	—	—
G	5'-D(PCPAPTPTPCPAPAPG)-3'	dna	8	—	—
A	Reverse transcriptase (EC 2.7.7.49)	protein	255	30% helix, 22% 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	178	0.49	0.76	24	empty

Interfaces

3 interfaces between chains.

B–G · 364 Å² buried · 39 hydrogen bonds · nucleic-nucleic
G–A · 209 Å² buried · 4 hydrogen bonds · protein-nucleic
B–A · 194 Å² buried · 5 hydrogen bonds · protein-nucleic

Compared structures

2FJW · d(CTTGAATGCATTCAAG) in complex with MMLV RT catalytic fragment · 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 2FJW · PDBe 2FJW · UniProt P03355

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