1R0A

Crystal structure of HIV-1 reverse transcriptase covalently tethered to DNA template-primer solved to 2.8 angstroms

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A (T)	5'-D(*A*TP*GP*CP*AP*TP*CP*GP*GP*CP*GP*CP*TP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*GP*GP*T)-3'	polymer	27	8367.4	1
2	B (P)	5'-D(*C*CP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*AP*GP*CP*GP*CP*CP*GP*(2DA))-3'	polymer	21	6360.1	1
3	C (A)	Reverse transcriptase	polymer	558	64249.7	1	UniProt (P03366) Pfam (PF00078) Pfam (PF06817) Pfam (PF06815) Pfam (PF00075)	Human immunodeficiency virus 1
4	D (B)	Reverse transcriptase	polymer	429	50152.6	1	UniProt (P03366) Pfam (PF00078) Pfam (PF06817) Pfam (PF06815)	Human immunodeficiency virus 1
5	E (L)	monoclonal antibody (light chain)	polymer	211	23362.7	1	Pfam (PF07654) UniProt (by SIFTS) (P01837)	Mus musculus (house mouse)
6	F (H)	monoclonal antibody (heavy chain)	polymer	225	24000.8	1	Pfam (PF07654) UniProt (by SIFTS) (P01868)	Mus musculus (house mouse)
7	G, I (P, B)	GLYCEROL	non-polymer		92.1	2	Chemie (GOL)
8	H (A)	MAGNESIUM ION	non-polymer		24.3	1	Chemie (MG)
9	J (H)	alpha-D-glucopyranose	non-polymer		180.2	1	Chemie (GLC)
10	K, L, M, N, O (T, A, B, L, H)	water	water		18.0	28	Chemie (HOH)

Sequence modifications

A: 1 - 558 (UniProt: P03366)

PDB	External Database	Details
Cys 258	Gln 425	engineered mutation
Ser 280	Cys 447	engineered mutation

B: 1 - 429 (UniProt: P03366)

PDB	External Database	Details
Ser 280	Cys 447	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	6
	Total formula weight	176493.3
Non-Polymers*	Number of molecules	4
	Total formula weight	388.6
All*	Total formula weight	176881.9

*Water molecules are not included.