eF-site ID 1bim-AB PDB Code 1bim Chain A, B click to enlarge Title CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS Classification HYDROLASE/HYDROLASE INHIBITOR Compound Renin Source (RENI_HUMAN) Sequence A:  GNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSN VWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRY STGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAE FDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYN RDSESLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMK GVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEAL GAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVF QESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTE FDRRNNRIGFALAR B:  GNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSN VWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRY STGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAE FDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYN RDSSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKG VSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALG AKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQ ESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEF DRRNNRIGFALAR Description Functional site 1) chain A residue 32 type sequence D description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 2) chain A residue 34 type sequence G description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 3) chain A residue 75 type sequence Y description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 4) chain A residue 76 type sequence S description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 5) chain A residue 77 type sequence T description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 6) chain A residue 111 type sequence P description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 7) chain A residue 117 type sequence F description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 8) chain A residue 215 type sequence D description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 9) chain A residue 217 type sequence G description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 10) chain A residue 218 type sequence A description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 11) chain A residue 219 type sequence S description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 12) chain A residue 220 type sequence Y description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 13) chain A residue 222 type sequence S description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 14) chain A residue 289 type sequence M description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 15) chain A residue 291 type sequence I description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 16) chain A residue 300 type sequence A description BINDING SITE FOR RESIDUE 0QB A 391 source : AC1 17) chain B residue 12 type sequence T description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 18) chain B residue 13 type sequence Q description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 19) chain B residue 32 type sequence D description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 20) chain B residue 75 type sequence Y description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 21) chain B residue 76 type sequence S description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 22) chain B residue 77 type sequence T description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 23) chain B residue 112 type sequence F description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 24) chain B residue 114 type sequence L description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 25) chain B residue 213 type sequence L description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 26) chain B residue 215 type sequence D description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 27) chain B residue 217 type sequence G description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 28) chain B residue 218 type sequence A description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 29) chain B residue 219 type sequence S description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 30) chain B residue 220 type sequence Y description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 31) chain B residue 222 type sequence S description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 32) chain B residue 291 type sequence I description BINDING SITE FOR RESIDUE 0QB B 391 source : AC2 33) chain A residue 29-40 type prosite sequence VVFDTGSSNVWV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VVFDTGSSNVWV source prosite : PS00141 34) chain A residue 212-223 type prosite sequence ALVDTGASYISG description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VVFDTGSSNVWV source prosite : PS00141 35) chain A residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:20927107 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 215 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:20927107 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:20927107 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 215 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:20927107 source Swiss-Prot : SWS_FT_FI1 39) chain A residue -1 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2493678 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 67 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2493678 source Swiss-Prot : SWS_FT_FI2 41) chain B residue -1 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2493678 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 67 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2493678 source Swiss-Prot : SWS_FT_FI2

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