eF-site ID 4dmx-A PDB Code 4dmx Chain A click to enlarge Title Cathepsin K inhibitor Classification Hydrolase/Hydrolase inhibitor Compound Cathepsin K Source Homo sapiens (Human) (CATK_HUMAN) Sequence A:  APDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKK KTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRG IDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKA LKRAVARVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNL NHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNK NNACGIANLASFPKM Description (1)  HUMAN CATHEPSIN K IN COMPLEX WITH AZCat2 Functional site 1) chain A residue 14 type sequence T description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 2) chain A residue 15 type sequence P description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 3) chain A residue 19 type sequence Q description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 4) chain A residue 23 type sequence G description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 5) chain A residue 24 type sequence S description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 6) chain A residue 25 type sequence C description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 7) chain A residue 26 type sequence W description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 8) chain A residue 59 type sequence E description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 9) chain A residue 61 type sequence D description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 10) chain A residue 64 type sequence G description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 11) chain A residue 65 type sequence G description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 12) chain A residue 66 type sequence G description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 13) chain A residue 67 type sequence Y description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 14) chain A residue 134 type sequence A description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 15) chain A residue 160 type sequence L description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 16) chain A residue 161 type sequence N description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 17) chain A residue 209 type sequence L description BINDING SITE FOR RESIDUE 0LB A 301 source : AC1 18) chain A residue 119 type sequence K description BINDING SITE FOR RESIDUE GOL A 302 source : AC2 19) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE GOL A 302 source : AC2 20) chain A residue 176 type sequence K description BINDING SITE FOR RESIDUE GOL A 302 source : AC2 21) chain A residue 198 type sequence R description BINDING SITE FOR RESIDUE GOL A 302 source : AC2 22) chain A residue 199 type sequence N description BINDING SITE FOR RESIDUE GOL A 302 source : AC2 23) chain A residue 25 type ACT_SITE sequence C description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 162 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 182 type ACT_SITE sequence N description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 19-30 type prosite sequence QGQCGSCWAFSS description THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSS source prosite : PS00139 27) chain A residue 160-170 type prosite sequence LNHAVLAVGYG description THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LNHAVLAVGYG source prosite : PS00639 28) chain A residue 177-196 type prosite sequence HWIIKNSWGENWGNKGYILM description THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. HWIiKNSWgenWGnkGYIlM source prosite : PS00640

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