eF-site ID 6qfe-AB PDB Code 6qfe Chain A, B click to enlarge Title Crystal Structure of Human Kallikrein 5 in complex with GSK144 Classification HYDROLASE Compound Kallikrein-5 Source (KLK5_HUMAN) Sequence A:  IINGSDCDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTA AHCRKKVFRVRLGHYSLSPVYESGQQMFQGVKSIPHPGYS HPGHSNDLMLIKLNRRIRPTKDVRPINVSSHCPSAGTKCL VSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYPRQID DTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPC ARPNRPGVYTNLCKFTKWIQETIQANS B:  IINGSDCDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTA AHCRKKVFRVRLGHYSLSPVYESGQQMFQGVKSIPHPGYS HPGHSNDLMLIKLNRRIRPTKDVRPINVSSHCPSAGTKCL VSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYPRQID DTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPC ARPNRPGVYTNLCKFTKWIQETIQANS Description Functional site 1) chain A residue 159 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17881000 source Swiss-Prot : SWS_FT_FI4 2) chain B residue 159 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17881000 source Swiss-Prot : SWS_FT_FI4 3) chain A residue 18 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 4) chain A residue 122 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 5) chain A residue 202 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 18 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 7) chain B residue 122 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 8) chain B residue 202 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 57 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:17881000 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 102 type ACT_SITE sequence D description Charge relay system => ECO:0000269|PubMed:17881000 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 195 type ACT_SITE sequence S description Charge relay system => ECO:0000269|PubMed:17881000 source Swiss-Prot : SWS_FT_FI1 12) chain B residue 57 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:17881000 source Swiss-Prot : SWS_FT_FI1 13) chain B residue 102 type ACT_SITE sequence D description Charge relay system => ECO:0000269|PubMed:17881000 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 195 type ACT_SITE sequence S description Charge relay system => ECO:0000269|PubMed:17881000 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 99 type SITE sequence H description Major binding site for inhibitory zinc source Swiss-Prot : SWS_FT_FI2 16) chain B residue 99 type SITE sequence H description Major binding site for inhibitory zinc source Swiss-Prot : SWS_FT_FI2 17) chain A residue 53-58 type prosite sequence LTAAHC description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC source prosite : PS00134 18) chain A residue 189-200 type prosite sequence DSCQGDSGGPVV description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV source prosite : PS00135

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