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7SJX

Cryo-EM Structure of the PR-RT components of the HIV-1 Pol Polyprotein

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003964molecular_functionRNA-directed DNA polymerase activity
A0004190molecular_functionaspartic-type endopeptidase activity
A0004521molecular_functionRNA endonuclease activity
A0004523molecular_functionRNA-DNA hybrid ribonuclease activity
A0006278biological_processRNA-templated DNA biosynthetic process
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
A0015074biological_processDNA integration
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003964molecular_functionRNA-directed DNA polymerase activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0004521molecular_functionRNA endonuclease activity
B0004523molecular_functionRNA-DNA hybrid ribonuclease activity
B0006278biological_processRNA-templated DNA biosynthetic process
B0006508biological_processproteolysis
B0008270molecular_functionzinc ion binding
B0015074biological_processDNA integration
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues82
DetailsZN_FING: Integrase-type => ECO:0000255|PROSITE-ProRule:PRU00450
ChainResidueDetails
AASP644-GLN685
BASP638-GLN679

site_idSWS_FT_FI2
Number of Residues94
DetailsDNA_BIND: Integrase-type => ECO:0000255|PROSITE-ProRule:PRU00506
ChainResidueDetails
APHE864-ASP911
BPHE858-ASP905

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029
ChainResidueDetails
AALA25
BALA25

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP204
AASP271
AASP272
BASP209
BASP284
BASP285

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP524
AGLU559
AASP579
AASP630
BASP518
BGLU553
BASP573
BASP624

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00450
ChainResidueDetails
AHIS653
AHIS657
ACYS681
ACYS684
BHIS647
BHIS651
BCYS675
BCYS678

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP705
AASP757
BASP699
BASP751

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04585
ChainResidueDetails
AGLU793
BGLU787

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Cleavage; by viral protease
ChainResidueDetails
APHE0
BPHE0

site_idSWS_FT_FI10
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE99

site_idSWS_FT_FI11
Number of Residues4
DetailsSITE: Essential for RT p66/p51 heterodimerization
ChainResidueDetails
ATRP482
ATRP495
BTRP476
BTRP489

site_idSWS_FT_FI12
Number of Residues2
DetailsSITE: Cleavage; by viral protease; partial
ChainResidueDetails
APHE521
BPHE515

site_idSWS_FT_FI13
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AASP641
BASP635

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PDB entries from 2024-11-06

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