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D(ATTTAGTTAACTAAAT) complexed with mmlv rt catalytic fragment

Analyse D(ATTTAGTTAACTAAAT) complexed 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: 2R2T
Type: protein + DNA
Length: 271 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA (5'-D(*DAP*DTP*DTP*DTP*DAP*DGP*DTP*DT)-3'); DNA…
EC: 2.7.7.49
UniProt: P03355
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 3 distinct chains · 31% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	DNA (5'-D(DAPDTPDTPDTPDAPDGPDTPDT)-3')	dna	8	—	—
G	DNA (5'-D(PDAPDAPDCPDTPDAPDAPDAPDT)-3')	dna	8	—	—
A	Reverse transcriptase (EC 2.7.7.49)	protein	255	31% helix, 24% strand	P03355

Pockets

2 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	237	0.54	0.76	26	empty
2	73	0.31	0.74	16	empty

Interfaces

3 interfaces between chains.

B–G · 339 Å² buried · 34 hydrogen bonds · nucleic-nucleic
B–A · 224 Å² buried · 4 hydrogen bonds · protein-nucleic
G–A · 193 Å² buried · 4 hydrogen bonds · protein-nucleic

Compared structures

2R2T · d(ATTTAGTTAACTAAAT) complexed 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 2R2T · PDBe 2R2T · UniProt P03355

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