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2AVS

kinetics, stability, and structural changes in high resolution crystal structures of HIV-1 protease with drug resistant mutations L24I, I50V, and G73S

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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 201
ChainResidue
APRO39
AGLY40
AHOH1149
AHOH1170
AHOH1269
AHOH1302
BMET36
BSER37

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ALYS55
AHOH1124
AHOH1157
AHOH1199
AHOH1244
AHOH1245
BHIS69
BLYS70
APRO1

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 703
ChainResidue
BPRO1
BARG57
BHIS69
BHOH1095
BHOH1134

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS B 401
ChainResidue
AGLY17
BLYS14
BGLY16
BGLY17
BILE63
BGLU65
BACY605

site_idAC5
Number of Residues39
DetailsBINDING SITE FOR RESIDUE MK1 B 902
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AILE47
AGLY48
AGLY49
AVAL50
APRO81
AVAL82
AHOH1307
BARG8
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BILE47
BGLY48
BGLY49
BPRO81
BVAL82
BILE84
BHOH1005
BHOH1011
BHOH1024
BHOH1032
BHOH1074
BHOH1120
BHOH1140
BHOH1144
BHOH1173
BHOH1182
BHOH1283

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ACY B 603
ChainResidue
ATHR4
ATRP6
AGLY51
AHOH1167
BTHR91
BGLY94
BHOH1006
BHOH1041
BHOH1077
BHOH1169

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY B 604
ChainResidue
BVAL11
BTHR12
BGLU21
BTRP42
BACY606
BHOH1152
BHOH1288

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY B 605
ChainResidue
ALYS14
AILE15
AGLY16
AGLY17
AILE63
AHOH1259
BDMS401
BHOH1308

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACY B 606
ChainResidue
BHOH1192
BHOH1241
BHOH1288
BVAL11
BTHR12
BTRP42
BALA67
BACY604
BHOH1152

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
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AILE64
BILE64

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AILE64
BILE64

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

222036

PDB entries from 2024-07-03

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