Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3CYX

Crystal structure of HIV-1 mutant I50V and inhibitor saquinavira

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 Residues34
DetailsBINDING SITE FOR RESIDUE ROC A 201
ChainResidue
AARG8
AVAL50
ATHR80
APRO81
AVAL82
AILE84
AGOL801
AHOH1004
AHOH1005
AHOH1068
AHOH1162
AASP25
BARG8
BASP25
BGLY27
BASP29
BASP30
BILE47
BGLY48
BGLY49
BVAL50
BTHR80
AGLY27
BPRO81
BILE84
BHOH1192
BHOH1209
BHOH1238
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AASP60
AHOH1078
AHOH1103
AHOH1135
AHOH1156
AHOH1235

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 601
ChainResidue
AMET46
AGOL801
BGLN61
BHOH1006

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 801
ChainResidue
AILE47
AGLY48
AROC201
AACY601
AHOH1049
AHOH1097
BPO4701

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 701
ChainResidue
AGOL801
BARG8
BHOH1163

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon