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4OBD

Crystal Structure of Nelfinavir-Resistant, Inactive HIV-1 Protease (D30N/N88D) in Complex with the p1-p6 substrate variant (L449F/S451N)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 101
ChainResidue
BLYS7
BARG8
BLEU10
BHOH212

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 102
ChainResidue
BGLN2
DGLU35
DARG57
DPRO79

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 101
ChainResidue
CGLU34
CVAL82
CASN83
CGLU21

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO E 101
ChainResidue
ALYS7
AARG8
BARG87
EARG9

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues276
DetailsDomain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Cleavage; by viral protease","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-11-05

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