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3ECG

High Resolution HIV-2 Protease Structure in Complex with Antiviral Inhibitor GRL-98065

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 Residues21
DetailsBINDING SITE FOR RESIDUE 065 A 201
ChainResidue
AASP25
AILE84
AHOH1017
AHOH1083
BASP125
BGLY127
BALA128
BASP129
BASP130
BILE132
BGLY148
AGLY27
BGLY149
BILE150
AALA28
AASP30
AILE32
AGLY48
AGLY49
APRO81
AILE82

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD A 304
ChainResidue
AGLN2
APHE3
ALEU99
AZN404
ACL509
BPRO101

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE IMD A 306
ChainResidue
ATYR14
AGLU16
AGLY17
AGLU63
AGLU65
AGLU65
AZN407
AZN411
AHOH1011

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AASP30
ACL503
AHOH1026
AHOH1027
AHOH1028

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 404
ChainResidue
ALEU99
AIMD304
ACL509
AHOH1007
AHOH1008

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 406
ChainResidue
AASP79
AHOH1032
AHOH1033
BGLU137

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 407
ChainResidue
AGLU65
AGLU65
AIMD306
AHOH1005
AHOH1005

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 411
ChainResidue
AGLU63
AGLU65
AIMD306
ACL507
AHOH1009
AHOH1011

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AASP30
AZN402
AHOH1026
BLYS157

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 507
ChainResidue
AGLU63
AGLU65
AASN68
ALYS69
AZN411

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 509
ChainResidue
ALEU99
AIMD304
AZN404
AHOH1008
AHOH1101

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 601
ChainResidue
AASN40
AASN41
APRO44
AHOH1067
AHOH1088
AHOH1104
BASN140

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD B 301
ChainResidue
BGLU121
BILE146
BASN155
BASP179
BIMD302
BZN401

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD B 302
ChainResidue
BGLU121
BPHE153
BASP179
BIMD301
BZN401
BHOH1169

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD B 303
ChainResidue
BCL502
BASP130
BILE146
BZN403
BZN410
BCL501

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD B 305
ChainResidue
APRO81
BTRP106
BZN405
BCL505
BCL506
BCL508
BHOH1062

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BGLU121
BASP179
BIMD301
BIMD302

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 403
ChainResidue
BASP130
BIMD303
BZN410
BCL502
BHOH1001

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 405
ChainResidue
BIMD305
BCL505
BCL506
BCL508

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 408
ChainResidue
BGLU165
BCL504
BHOH1002
BHOH1003

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 409
ChainResidue
BGLU158
BHOH1010
BHOH1113
BHOH1144

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 410
ChainResidue
BASP130
BIMD303
BZN403
BHOH1001
BHOH1004

site_idCC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B 501
ChainResidue
BTHR112
BLYS145
BILE146
BIMD303
BHOH1053
BHOH1092

site_idCC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 502
ChainResidue
BLYS107
BGLY148
BIMD303
BZN403

site_idCC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 504
ChainResidue
BZN408
BHOH1003

site_idCC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CL B 505
ChainResidue
BSER104
BLEU105
BTRP106
BLYS107
BIMD305
BZN405
BCL506
BCL508

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 506
ChainResidue
BIMD305
BZN405
BCL505

site_idDC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 508
ChainResidue
AARG8
BIMD305
BZN405
BCL505

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLLDTGADDSIV
ChainResidueDetails
AVAL22-VAL33

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
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
ALEU99
BLEU199

220472

PDB entries from 2024-05-29

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