eF-site ID 1gnn-AB PDB Code 1gnn Chain A, B click to enlarge Title HIV-1 PROTEASE MUTANT WITH VAL 82 REPLACED BY ASN (V82N) COMPLEXED WITH U89360E (INHIBITOR) Classification HYDROLASE (ACID PROTEASE) Compound HIV-1 PROTEASE Source (POL_HV1PV) Sequence A:  PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG RWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPT PNNIIGRNLLTQIGCTLNF B:  PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG RWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPT PNNIIGRNLLTQIGCTLNF Description Functional site 1) chain A residue 8 type sequence R description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 2) chain A residue 25 type sequence D description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 3) chain A residue 27 type sequence G description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 4) chain A residue 49 type sequence G description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 5) chain A residue 50 type sequence I description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 6) chain A residue 82 type sequence N description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 7) chain A residue 84 type sequence I description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 8) chain B residue 23 type sequence L description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 9) chain B residue 25 type sequence D description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 10) chain B residue 27 type sequence G description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 11) chain B residue 28 type sequence A description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 12) chain B residue 29 type sequence D description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 13) chain B residue 30 type sequence D description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 14) chain B residue 47 type sequence I description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 15) chain B residue 48 type sequence G description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 16) chain B residue 49 type sequence G description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 17) chain B residue 50 type sequence I description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 18) chain B residue 81 type sequence P description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 19) chain B residue 82 type sequence N description BINDING SITE FOR RESIDUE U0E A 100 source : AC1 20) chain A residue 25 type sequence D description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 21) chain A residue 27 type sequence G description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 22) chain A residue 28 type sequence A description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 23) chain A residue 29 type sequence D description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 24) chain A residue 30 type sequence D description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 25) chain A residue 47 type sequence I description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 26) chain A residue 48 type sequence G description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 27) chain A residue 49 type sequence G description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 28) chain A residue 50 type sequence I description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 29) chain A residue 81 type sequence P description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 30) chain A residue 82 type sequence N description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 31) chain A residue 84 type sequence I description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 32) chain B residue 25 type sequence D description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 33) chain B residue 27 type sequence G description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 34) chain B residue 49 type sequence G description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 35) chain B residue 50 type sequence I description BINDING SITE FOR RESIDUE U0E A 101 source : AC2 36) chain A residue 99 type SITE sequence F description Cleavage; by viral protease => ECO:0000269|PubMed:2476069 source Swiss-Prot : SWS_FT_FI3 37) chain B residue 99 type SITE sequence F description Cleavage; by viral protease => ECO:0000269|PubMed:2476069 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 64 type MOD_RES sequence I description Phosphotyrosine; by host => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 39) chain B residue 64 type MOD_RES sequence I description Phosphotyrosine; by host => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 40) chain A 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 41) 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 42) chain A residue 64 type SITE sequence I description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 64 type SITE sequence I description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 22-33 type prosite sequence ALLDTGADDTVL description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL source prosite : PS00141

Display surface Download Links