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6DJ5

HIV-1 protease with mutation L76V in complex with GRL-0519 (tris-tetrahydrofuran as P2 ligand)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue NA A 101
ChainResidue
AASP60
AHOH201
AHOH218
AHOH231

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 102
ChainResidue
ATHR74
AASN88
BARG41

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 103
ChainResidue
AHOH227
BGLN61
BGLN92
BHOH1118
BHOH1132
ALYS45
AMET46

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 104
ChainResidue
ALYS14
AILE15
AGLY16
AGLY17
AILE63
ALYS70

site_idAC5
Number of Residues31
Detailsbinding site for residue G52 B 201
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH206
AHOH245
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH1102
BHOH1124
BHOH1142
BHOH1147

site_idAC6
Number of Residues4
Detailsbinding site for residue NA B 202
ChainResidue
BASP60
BGOL208
BHOH1123
BHOH1155

site_idAC7
Number of Residues2
Detailsbinding site for residue CL B 203
ChainResidue
BTRP6
BPRO44

site_idAC8
Number of Residues4
Detailsbinding site for residue CL B 204
ChainResidue
BGLY73
BTHR74
BASN88
BHOH1131

site_idAC9
Number of Residues1
Detailsbinding site for residue CL B 205
ChainResidue
BTHR12

site_idAD1
Number of Residues2
Detailsbinding site for residue CL B 206
ChainResidue
BLYS7
BARG8

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL B 207
ChainResidue
ATRP6
BASP29
BARG87
BASN88
BHOH1122
BHOH1133

site_idAD3
Number of Residues8
Detailsbinding site for residue GOL B 208
ChainResidue
BARG41
BLYS43
BGLN58
BTYR59
BASP60
BNA202
BHOH1101
BHOH1123

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000305|PubMed:33542150
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 175
ChainResidueDetails
AASP25hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ATHR26electrostatic stabiliser, transition state stabiliser
AGLY27electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 175
ChainResidueDetails
BASP25hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BTHR26electrostatic stabiliser, transition state stabiliser
BGLY27electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-06-12

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