eF-site ID 1qtn-AB PDB Code 1qtn Chain A, B click to enlarge Title CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE Classification HYDROLASE/HYDROLASE INHIBITOR Compound CASPASE-8 Source Homo sapiens (Human) (1QTN) Sequence A:  DKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNG THLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLM DHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTG LKCPSLAGKPKVFFIQACQGDNYQKGIPVETD B:  TRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSL RERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFT LRKKLVFPSD Description Functional site 1) chain A residue 334 type sequence Y description BINDING SITE FOR RESIDUE DTD B 505 source : AC1 2) chain A residue 337 type sequence T description BINDING SITE FOR RESIDUE DTD B 505 source : AC1 3) chain B residue 396 type sequence E description BINDING SITE FOR RESIDUE DTD B 505 source : AC1 4) chain B residue 399 type sequence F description BINDING SITE FOR RESIDUE DTD B 505 source : AC1 5) chain B residue 401 type sequence L description BINDING SITE FOR RESIDUE DTD B 505 source : AC1 6) chain B residue 469 type sequence T description BINDING SITE FOR RESIDUE DTD B 505 source : AC1 7) chain A residue 231 type sequence K description BINDING SITE FOR RESIDUE DTD A 506 source : AC2 8) chain A residue 232 type sequence P description BINDING SITE FOR RESIDUE DTD A 506 source : AC2 9) chain A residue 278 type sequence H description BINDING SITE FOR RESIDUE DTD A 506 source : AC2 10) chain A residue 290 type sequence E description BINDING SITE FOR RESIDUE DTD A 506 source : AC2 11) chain A residue 294 type sequence E description BINDING SITE FOR RESIDUE DTD A 506 source : AC2 12) chain A residue 260 type sequence R description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 13) chain A residue 317 type sequence H description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 14) chain A residue 318 type sequence G description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 15) chain A residue 358 type sequence Q description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 16) chain A residue 360 type sequence C description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 17) chain B residue 411 type sequence S description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 18) chain B residue 412 type sequence Y description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 19) chain B residue 413 type sequence R description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 20) chain B residue 415 type sequence P description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 21) chain B residue 420 type sequence W description BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE source : AC3 22) chain A residue 258 type catalytic sequence R description 818 source MCSA : MCSA1 23) chain A residue 317 type catalytic sequence H description 818 source MCSA : MCSA1 24) chain A residue 318 type catalytic sequence G description 818 source MCSA : MCSA1 25) chain A residue 360 type catalytic sequence C description 818 source MCSA : MCSA1 26) chain A residue 304-318 type prosite sequence HSNMDCFICCILSHG description CASPASE_HIS Caspase family histidine active site. HsnmdCfiCcILSHG source prosite : PS01121 27) chain A residue 351-362 type prosite sequence KPKVFFIQACQG description CASPASE_CYS Caspase family cysteine active site. KPKVFFIQACQG source prosite : PS01122 28) chain A residue 360 type MOD_RES sequence C description Phosphoserine; by CDK1 => ECO:0000269|PubMed:20937773 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 413 type MOD_RES sequence R description (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 374 type SITE sequence D description Cleavage; by CASP6 => ECO:0000269|PubMed:22858542 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O89110 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 334 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI6

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