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5DGW

Crystal Structure of HIV-1 Protease Inhibitor GRL-105-11A Containing Substituted fused-Tetrahydropyranyl 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 Residues29
Detailsbinding site for residue 5B5 A 201
ChainResidue
AASP25
APRO81
AVAL82
AHOH1001
AHOH1003
AHOH1010
AHOH1025
AHOH1034
BASP25
BGLY27
BALA28
AGLY27
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH1111
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49
AILE50

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 202
ChainResidue
AASP60
AHOH1018
AHOH1019
AHOH1028
AHOH1039
AHOH1045

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 203
ChainResidue
ATHR74
AASN88
BARG41

site_idAC4
Number of Residues1
Detailsbinding site for residue CL B 101
ChainResidue
BTRP6

site_idAC5
Number of Residues3
Detailsbinding site for residue CL B 102
ChainResidue
BTHR74
BASN88
BHOH1126

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 2024-10-09

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