eF-site ID 3hha-A PDB Code 3hha Chain A 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 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 A residue 66 type sequence N description BINDING SITE FOR RESIDUE ACT A 222 source : AC3 21) chain A residue 162 type sequence D description BINDING SITE FOR RESIDUE ACT A 222 source : AC3 22) 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 23) chain A residue 163 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI2 24) chain A residue 187 type ACT_SITE sequence N description source Swiss-Prot : SWS_FT_FI2 25) chain A residue 25 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:9468501 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 19-30 type prosite sequence QGQCGSCWAFSA description THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSA source prosite : PS00139 27) chain A residue 161-171 type prosite sequence MDHGVLVVGYG description THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. MDHGVLVVGYG source prosite : PS00639 28) 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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