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2HNZ

Crystal Structure of E138K Mutant HIV-1 Reverse Transcriptase in Complex with PETT-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003964molecular_functionRNA-directed DNA polymerase activity
A0004523molecular_functionRNA-DNA hybrid ribonuclease activity
A0006278biological_processRNA-templated DNA biosynthetic process
B0003964molecular_functionRNA-directed DNA polymerase activity
B0006278biological_processRNA-templated DNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 1300
ChainResidue
AGLY436
AARG461

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 1301
ChainResidue
AGLY436
AALA437
AASN460
AARG461
BLYS82
BALA288

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PC0 A 999
ChainResidue
ALYS103
AVAL179
ATYR181
ATYR188
APHE227
ALEU234
AHIS235
ATYR318
ALYS101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
BVAL111
BLEU187
ALEU187

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BASP186
BASP110
BASP185

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Essential for RT p66/p51 heterodimerization
ChainResidueDetails
BTRP402
BGLU415

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Essential for RT p66/p51 heterodimerization => ECO:0000250
ChainResidueDetails
BTRP401
BTRP414

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by viral protease; partial => ECO:0000250
ChainResidueDetails
ATYR441

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 175
ChainResidueDetails

222415

PDB entries from 2024-07-10

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