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6DJ7

HIV-1 protease with mutation L76V in complex with GRL-5010 (gem-difluoro-bis-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 Residues6
Detailsbinding site for residue NA A 501
ChainResidue
AASP60
AHOH619
AHOH629
AHOH639
AHOH648
AHOH661

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 502
ChainResidue
ATHR74
AASN88
BARG41

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 503
ChainResidue
ALYS55
AHOH645
BILE63

site_idAC4
Number of Residues32
Detailsbinding site for residue G10 B 201
ChainResidue
ALEU23
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH602
AHOH618
BARG8
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BPRO81
BILE84
BHOH312
BHOH324
BHOH366
BHOH385

site_idAC5
Number of Residues2
Detailsbinding site for residue CL B 202
ChainResidue
BTRP6
BACT206

site_idAC6
Number of Residues3
Detailsbinding site for residue CL B 203
ChainResidue
BTHR74
BASN88
BHOH345

site_idAC7
Number of Residues8
Detailsbinding site for residue GOL B 204
ChainResidue
AGLN18
AMET36
ASER37
BTHR12
BGLU65
BALA67
BGLY68
BHOH352

site_idAC8
Number of Residues5
Detailsbinding site for residue ACT B 205
ChainResidue
BPRO39
BGLY40
BARG41
BTYR59
BASP60

site_idAC9
Number of Residues5
Detailsbinding site for residue ACT B 206
ChainResidue
BTHR4
BPRO44
BCL202
BHOH313
BHOH381

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 2024-05-22

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