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1JLG

CRYSTAL STRUCTURE OF Y188C MUTANT HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH UC-781

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 Residues10
DetailsBINDING SITE FOR RESIDUE UC1 A 999
ChainResidue
ALEU100
ATYR318
ALYS101
AVAL179
ATYR181
ACSD188
AGLY190
APHE227
ALEU234
APRO236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BVAL111
BASP186
BLEU187

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
BPRO1
ASER499

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Essential for RT p66/p51 heterodimerization => ECO:0000250
ChainResidueDetails
BTRP402
BGLU415

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APRO1

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Essential for RT p66/p51 heterodimerization => ECO:0000250
ChainResidueDetails
ATRP402
AGLU415

site_idSWS_FT_FI6
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

217705

PDB entries from 2024-03-27

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