eF-site ID 1a9m-B PDB Code 1a9m Chain B click to enlarge Title G48H MUTANT OF HIV-1 PROTEASE IN COMPLEX WITH A PEPTIDIC INHIBITOR U-89360E Classification ASPARTYL PROTEASE Compound HIV-1 PROTEASE Source (POL_HV1PV) Sequence B:  PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG RWKPKMIHGIGGFIKVRQYDQILIEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF Description Functional site 1) chain B residue 23 type sequence L description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 2) chain B residue 25 type sequence D description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 3) chain B residue 27 type sequence G description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 4) chain B residue 28 type sequence A description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 5) chain B residue 29 type sequence D description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 6) chain B residue 30 type sequence D description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 7) chain B residue 47 type sequence I description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 8) chain B residue 48 type sequence H description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 9) chain B residue 49 type sequence G description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 10) chain B residue 50 type sequence I description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 11) chain B residue 82 type sequence V description BINDING SITE FOR RESIDUE U0E B 100 source : AC1 12) chain B residue 99 type SITE sequence F description Cleavage; by viral protease => ECO:0000269|PubMed:2476069 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 64 type MOD_RES sequence I description Phosphotyrosine; by host => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 14) chain B residue 25 type ACT_SITE sequence D description For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 64 type SITE sequence I description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI2

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