eF-site ID 1zpk-AB PDB Code 1zpk Chain A, B click to enlarge Title Crystal structure of the complex of mutant HIV-1 protease (A71V, V82T, I84V) with a hydroxyethylamine peptidomimetic inhibitor BOC-PHE-PSI[R-CH(OH)CH2NH]-PHE-GLU-PHE-NH2 Classification HYDROLASE/HYDROLASE INHIBITOR Compound PROTEASE RETROPEPSIN Source Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) (POL_HV1BR) Sequence A:  PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG RWKPKMIGGIGGFIKVRQYDQILIEIXGHKVIGTVLVGPT PTNVIGRNLLTQIGCTLNF B:  PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG RWKPKMIGGIGGFIKVRQYDQILIEIXGHKVIGTVLVGPT PTNVIGRNLLTQIGCTLNF Description Functional site 1) chain A residue 8 type sequence R description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 2) chain A residue 23 type sequence L description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 3) chain A residue 25 type sequence D description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 4) chain A residue 27 type sequence G description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 5) chain A residue 28 type sequence A description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 6) chain A residue 29 type sequence D description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 7) chain A residue 30 type sequence D description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 8) chain A residue 47 type sequence I description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 9) chain A residue 48 type sequence G description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 10) chain A residue 49 type sequence G description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 11) chain A residue 50 type sequence I description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 12) chain A residue 53 type sequence F description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 13) chain A residue 81 type sequence P description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 14) chain A residue 82 type sequence T description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 15) chain B residue 123 type sequence L description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 16) chain B residue 125 type sequence D description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 17) chain B residue 127 type sequence G description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 18) chain B residue 128 type sequence A description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 19) chain B residue 129 type sequence D description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 20) chain B residue 130 type sequence D description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 21) chain B residue 147 type sequence I description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 22) chain B residue 148 type sequence G description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 23) chain B residue 149 type sequence G description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 24) chain B residue 150 type sequence I description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 25) chain B residue 181 type sequence P description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 26) chain B residue 182 type sequence T description BINDING SITE FOR RESIDUE 0ZS A 201 source : AC1 27) chain B residue 173 type sequence G description BINDING SITE FOR RESIDUE CL B 501 source : AC2 28) chain B residue 174 type sequence T description BINDING SITE FOR RESIDUE CL B 501 source : AC2 29) chain B residue 188 type sequence N description BINDING SITE FOR RESIDUE CL B 501 source : AC2 30) chain B residue 130 type sequence D description BINDING SITE FOR RESIDUE NA B 502 source : AC3 31) chain A residue 22-33 type prosite sequence ALLDTGADDTVL description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL source prosite : PS00141 32) chain A residue 64 type SITE sequence I description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 164 type SITE sequence I description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 64 type MOD_RES sequence I description Phosphotyrosine; by host => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 164 type MOD_RES sequence I description Phosphotyrosine; by host => ECO:0000250 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links