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2I0D

Crystal structure of AD-81 complexed with wild type HIV-1 protease

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 Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
AGLY68
AHIS69
ALYS70
BPRO1

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 502
ChainResidue
BHOH517
BHOH557
BHOH569
AARG14
AGLY16
AGLY17
AHOH516
BGLY16

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 503
ChainResidue
AMET36
AASN37
AHOH543
AHOH572
BPRO39
BGLY40
BHOH560

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 504
ChainResidue
ALYS20
AGLU21
AASN83
AHOH530
AHOH573
AHOH591

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 505
ChainResidue
AMUT200
BARG8

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE MUT A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AGLY48
AILE50
AVAL82
AHOH506
AHOH510
AHOH511
BARG8
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BPRO81
BVAL82
BILE84
BACT505
BHOH571

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

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

221716

PDB entries from 2024-06-26

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