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3ST5

Crystal structure of wild-type HIV-1 protease with C3-Substituted Hexahydrocyclopentafuranyl Urethane as P2-Ligand, GRL-0489A

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 511
ChainResidue
ATHR74
AASN88
BARG41

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE G89 B 201
ChainResidue
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH1002
BHOH1021
BHOH1025
ALEU23
AASP25
AGLY27
AALA28
AASP29
AASP30

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 512
ChainResidue
BTRP6

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
ChainResidueDetails
AASP25
BASP25

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

221716

PDB entries from 2024-06-26

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