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5HVP

CRYSTALLOGRAPHIC ANALYSIS OF A COMPLEX BETWEEN HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 PROTEASE AND ACETYL-PEPSTATIN AT 2.0-ANGSTROMS RESOLUTION

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 Residues2
DetailsBINDING SITE FOR RESIDUE CL A 343
ChainResidue
ATHR74
AASN88

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 336
ChainResidue
BGLY273
BTHR274
BASN288
BHOH356

site_idAC3
Number of Residues30
DetailsBINDING SITE FOR CHAIN C OF ACETYL-*PEPSTATIN
ChainResidue
AALA28
AASP29
AASP30
ALYS45
AILE47
AGLY48
AGLY49
AILE50
AVAL82
AILE84
BARG208
BLEU223
BASP225
BGLY227
BALA228
BASP229
BASP230
BLYS245
BILE247
BGLY248
BGLY249
BILE250
BILE284
BHOH319
CHOH308
CHOH311
CHOH417
AARG8
AASP25
AGLY27

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

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
BASP225

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE299

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BTHR226
BASP225

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP225

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PDB entries from 2024-07-24

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