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PDBsum entry 7lrm

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protein dna_rna ligands metals Protein-protein interface(s) links
Transferase/DNA PDB id
7lrm

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
553 a.a.
415 a.a.
DNA/RNA
Ligands
GLC-FRU ×2
SO4 ×2
GOL ×12
DCP ×2
Metals
_CA ×2
Waters ×150
PDB id:
7lrm
Name: Transferase/DNA
Title: Structure of HIV-1 reverse transcriptase in complex with DNA, dctp, and ca(2+) ion
Structure: Reverse transcriptase p66. Chain: a, c. Engineered: yes. Mutation: yes. Reverse transcriptase p51. Chain: b, d. Engineered: yes. Mutation: yes. DNA/RNA (38-mer).
Source: Human immunodeficiency virus type 1. HIV-1. Organism_taxid: 11676. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic construct. Organism_taxid: 32630
Resolution:
3.14Å     R-factor:   0.196     R-free:   0.244
Authors: A.Hoang,F.X.Ruiz,E.Arnold
Key ref: F.X.Ruiz et al. Structural basis of HIV inhibition by l-Nucleotides: opportunities for drug development and repurposing. To be published, . PubMed id: 35218925
Date:
16-Feb-21     Release date:   23-Feb-22    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P03366  (POL_HV1B1) -  Gag-Pol polyprotein from Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1447 a.a.
553 a.a.*
Protein chains
Pfam   ArchSchema ?
P03366  (POL_HV1B1) -  Gag-Pol polyprotein from Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1447 a.a.
415 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DNA/RNA chains
  T-G-C-OMC-C-OMC-C-C-C-T-T-C-G-G-T-G-C-T-T-T-G-C-A-C-C-G-A-A-G-G-G-G-G-G-G 35 bases
  T-G-C-OMC-C-OMC-C-C-C-T-T-C-G-G-T-G-C-T-T-T-G-C-A-C-C-G-A-A-G-G-G-G-G-G-G 35 bases

 Enzyme reactions 
   Enzyme class 1: Chains A, B, C, D: E.C.2.7.7.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 2: Chains A, B, C, D: E.C.2.7.7.49  - RNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
DNA(n)
+ 2'-deoxyribonucleoside 5'-triphosphate
= DNA(n+1)
+ diphosphate
   Enzyme class 3: Chains A, B, C, D: E.C.2.7.7.7  - DNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
DNA(n)
+ 2'-deoxyribonucleoside 5'-triphosphate
= DNA(n+1)
+ diphosphate
   Enzyme class 4: Chains A, B, C, D: E.C.3.1.-.-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 5: Chains A, B, C, D: E.C.3.1.13.2  - exoribonuclease H.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Exonucleolytic cleavage to 5'-phosphomonoester oligonucleotides in both 5'- to 3'- and 3'- to 5'-directions.
   Enzyme class 6: Chains A, B, C, D: E.C.3.1.26.13  - retroviral ribonuclease H.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 7: Chains A, B, C, D: E.C.3.4.23.16  - HIV-1 retropepsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 

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