Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1T05

HIV-1 reverse transcriptase crosslinked to template-primer with tenofovir-diphosphate bound as the incoming nucleotide substrate

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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 600
ChainResidue
AASP110
AVAL111
AASP185
ATNV823

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AASP443
AASP498

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TNV A 823
ChainResidue
AVAL111
AGLY112
AASP113
AALA114
AGLN151
AASP185
ALYS219
AMG600
PDDG822
TDT705
TDC706
ALYS65
AARG72
AASP110

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 824
ChainResidue
ALYS101
ALYS103
AVAL106
ATYR188
AHIS235
APRO236
ATYR318
AHOH827

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 825
ChainResidue
AGLU328
AGLN340
ATYR342
APRO345
AGOL826
AHOH829

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 826
ChainResidue
AGLN330
AGLN340
AGOL825

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 438
ChainResidue
BASP76
BARG78
BGLU79
BLYS82
BGLU413
BGOL439

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 439
ChainResidue
BGOL438

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsZN_FING: CCHC-type 1 => ECO:0000255|PROSITE-ProRule:PRU00047
ChainResidueDetails
BHIS235-TRP252

site_idSWS_FT_FI2
Number of Residues17
DetailsZN_FING: CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047
ChainResidueDetails
BASP256-GLY273

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000305|PubMed:33542150
ChainResidueDetails
BARG358

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BASP110
BASP185
BASP186

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA
ChainResidueDetails
BLYS66

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
BHIS208
BGLN222
BGLY285

site_idSWS_FT_FI7
Number of Residues3
DetailsSITE: Cleavage; by viral protease => ECO:0000255
ChainResidueDetails
BLYS238
BTYR271
BARG277

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Cleavage; by viral protease => ECO:0000305|PubMed:15183348
ChainResidueDetails
BGLY333
AGLY333

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Essential for RT p66/p51 heterodimerization => ECO:0000250
ChainResidueDetails
BTRP401
BTRP414

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034
ChainResidueDetails
ALYS220
AGLN242

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 175
ChainResidueDetails
BARG358hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLY359electrostatic stabiliser, transition state stabiliser
BALA360electrostatic stabiliser, hydrogen bond donor

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon