eF-site ID 3hha-ABCD PDB Code 3hha Chain A, B, C, D click to enlarge Title Crystal structure of cathepsin L in complex with AZ12878478 Classification HYDROLASE Compound Cathepsin L1 Source Homo sapiens (Human) (CATL1_HUMAN) Sequence A:  APRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFR KTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDN GGLDSEESYPYEATEESCKYNPKYSVANDAGFVDIPKQEK ALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSED MDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVK MAKDRRNHCGIASAASYPTV B:  APRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFR KTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDN GGLDSEESYPYEATEESCKYNPKYSVANDAGFVDIPKQEK ALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSED MDHGVLVVGYGFESTNKYWLVKNSWGEEWGMGGYVKMAKD RRNHCGIASAASYPTV C:  APRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFR KTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDN GGLDSEESYPYEATEESCKYNPKYSVANDAGFVDIPKQEK ALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSED MDHGVLVVGYGFNKYWLVKNSWGEEWGMGGYVKMAKDRRN HCGIASAASYPTV D:  APRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFR KTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDN GGLDSEESYPYEATEESCKYNPKYSVANDAGFVDIPKQEK ALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSED MDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVK MAKDRRNHCGIASAASYPTV Description Functional site 1) chain A residue 19 type sequence Q description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 2) chain A residue 23 type sequence G description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 3) chain A residue 24 type sequence S description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 4) chain A residue 25 type sequence C description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 5) chain A residue 26 type sequence W description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 6) chain A residue 61 type sequence G description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 7) chain A residue 67 type sequence G description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 8) chain A residue 68 type sequence G description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 9) chain A residue 69 type sequence L description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 10) chain A residue 70 type sequence M description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 11) chain A residue 135 type sequence A description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 12) chain A residue 161 type sequence M description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 13) chain A residue 162 type sequence D description BINDING SITE FOR RESIDUE NOW A 301 source : AC1 14) chain A residue 19 type sequence Q description BINDING SITE FOR RESIDUE PG4 A 221 source : AC2 15) chain A residue 20 type sequence G description BINDING SITE FOR RESIDUE PG4 A 221 source : AC2 16) chain A residue 21 type sequence Q description BINDING SITE FOR RESIDUE PG4 A 221 source : AC2 17) chain A residue 22 type sequence C description BINDING SITE FOR RESIDUE PG4 A 221 source : AC2 18) chain A residue 23 type sequence G description BINDING SITE FOR RESIDUE PG4 A 221 source : AC2 19) chain A residue 189 type sequence W description BINDING SITE FOR RESIDUE PG4 A 221 source : AC2 20) chain C residue 141 type sequence E description BINDING SITE FOR RESIDUE PG4 A 221 source : AC2 21) chain A residue 66 type sequence N description BINDING SITE FOR RESIDUE ACT A 222 source : AC3 22) chain A residue 162 type sequence D description BINDING SITE FOR RESIDUE ACT A 222 source : AC3 23) chain B residue 19 type sequence Q description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 24) chain B residue 23 type sequence G description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 25) chain B residue 24 type sequence S description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 26) chain B residue 25 type sequence C description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 27) chain B residue 26 type sequence W description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 28) chain B residue 61 type sequence G description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 29) chain B residue 63 type sequence E description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 30) chain B residue 67 type sequence G description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 31) chain B residue 68 type sequence G description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 32) chain B residue 69 type sequence L description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 33) chain B residue 135 type sequence A description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 34) chain B residue 161 type sequence M description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 35) chain B residue 162 type sequence D description BINDING SITE FOR RESIDUE NOW B 301 source : AC4 36) chain B residue 19 type sequence Q description BINDING SITE FOR RESIDUE PGE B 221 source : AC5 37) chain B residue 20 type sequence G description BINDING SITE FOR RESIDUE PGE B 221 source : AC5 38) chain B residue 22 type sequence C description BINDING SITE FOR RESIDUE PGE B 221 source : AC5 39) chain B residue 23 type sequence G description BINDING SITE FOR RESIDUE PGE B 221 source : AC5 40) chain B residue 144 type sequence L description BINDING SITE FOR RESIDUE PGE B 221 source : AC5 41) chain B residue 189 type sequence W description BINDING SITE FOR RESIDUE PGE B 221 source : AC5 42) chain C residue 19 type sequence Q description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 43) chain C residue 23 type sequence G description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 44) chain C residue 24 type sequence S description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 45) chain C residue 25 type sequence C description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 46) chain C residue 26 type sequence W description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 47) chain C residue 61 type sequence G description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 48) chain C residue 67 type sequence G description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 49) chain C residue 68 type sequence G description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 50) chain C residue 69 type sequence L description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 51) chain C residue 135 type sequence A description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 52) chain C residue 161 type sequence M description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 53) chain C residue 162 type sequence D description BINDING SITE FOR RESIDUE NOW C 301 source : AC6 54) chain D residue 19 type sequence Q description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 55) chain D residue 23 type sequence G description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 56) chain D residue 24 type sequence S description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 57) chain D residue 25 type sequence C description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 58) chain D residue 26 type sequence W description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 59) chain D residue 61 type sequence G description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 60) chain D residue 67 type sequence G description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 61) chain D residue 68 type sequence G description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 62) chain D residue 69 type sequence L description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 63) chain D residue 135 type sequence A description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 64) chain D residue 161 type sequence M description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 65) chain D residue 162 type sequence D description BINDING SITE FOR RESIDUE NOW D 301 source : AC7 66) chain D residue 17 type sequence K description BINDING SITE FOR RESIDUE GOL D 221 source : AC8 67) chain D residue 18 type sequence N description BINDING SITE FOR RESIDUE GOL D 221 source : AC8 68) chain D residue 86 type sequence E description BINDING SITE FOR RESIDUE GOL D 221 source : AC8 69) chain A residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI3 70) chain B residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI3 71) chain C residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI3 72) chain D residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI3 73) chain A residue 163 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI2 74) chain A residue 187 type ACT_SITE sequence N description source Swiss-Prot : SWS_FT_FI2 75) chain B residue 163 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI2 76) chain B residue 187 type ACT_SITE sequence N description source Swiss-Prot : SWS_FT_FI2 77) chain C residue 163 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI2 78) chain C residue 187 type ACT_SITE sequence N description source Swiss-Prot : SWS_FT_FI2 79) chain D residue 163 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI2 80) chain D residue 187 type ACT_SITE sequence N description source Swiss-Prot : SWS_FT_FI2 81) chain A residue 25 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:9468501 source Swiss-Prot : SWS_FT_FI1 82) chain B residue 25 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:9468501 source Swiss-Prot : SWS_FT_FI1 83) chain C residue 25 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:9468501 source Swiss-Prot : SWS_FT_FI1 84) chain D residue 25 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:9468501 source Swiss-Prot : SWS_FT_FI1 85) chain A residue 19-30 type prosite sequence QGQCGSCWAFSA description THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSA source prosite : PS00139 86) chain A residue 161-171 type prosite sequence MDHGVLVVGYG description THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. MDHGVLVVGYG source prosite : PS00639 87) chain A residue 182-201 type prosite sequence YWLVKNSWGEEWGMGGYVKM description THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgeeWGmgGYVkM source prosite : PS00640

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