eF-site ID 1nu9-ACDF PDB Code 1nu9 Chain A, C, D, F click to enlarge Title Staphylocoagulase-Prethrombin-2 complex Classification HYDROLASE/HYDROLASE INHIBITOR Compound Thrombin light and heavy chains Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  GEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAE IGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYP PWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHP RYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAAS LLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIV ERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGP FVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKK WIQKVIDQFG C:  IVTKDYSKESRVNENSKYGTLISDWYLKGRLTSLESQFIN ALGILETYHYGEKEYKDAKDKLMTRILGEDQYLLERKKVQ YEEYKKLYKKYKEENPTSKVKMKTFDQYTIEDLTMREYNE LTESLKSAVKDFEKDVEIIENQHHDLKPFTDEMEEKATAR VDDLANKAYSVYFAFVRDTQHKTEALELKAKVDLVLGDED KPHRISNERIEKEMIKDLESIIEDFFIETGLNKPDNITSY DSSKHHYKNHSEGFEALVKETREAVTNANDSWKTKTVKKY G D:  GEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAE IGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYP PWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHP RYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAAS LLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIV ERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGP FVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKK WIQKVIDQFG F:  IVTKDYSKESRVNENSKYGTLISDWYLKGRLTSLESQFIN ALGILETYHYGEKEYKDAKDKLMTRILGEDQYLLERKKVQ YEEYKKLYKKYKEENPTSKVKMKTFDQYTIEDLTMREYNE LTESLKSAVKDFEKDVEIIENQHHDLKPFTDEMEEKATAR VDDLANKAYSVYFAFVRDTQHKTEALELKAKVDLVLGDED KPHRISNERIEKEMIKDLESIIEDFFIETGLNKPDNITSY DSSKHHYKNHSEGFEALVKETREAVTNANDSWKTKTVKKY G Description (1)  Thrombin light and heavy chains (E.C.3.4.21.5)/Staphylocoagulase Functional site 1) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 2) chain A residue 60 type sequence L description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 3) chain A residue 60 type sequence L description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 4) chain A residue 99 type sequence L description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 5) chain A residue 174 type sequence I description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 6) chain A residue 189 type sequence D description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 7) chain A residue 190 type sequence A description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 8) chain A residue 193 type sequence G description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 9) chain A residue 195 type sequence S description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 10) chain A residue 214 type sequence S description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 11) chain A residue 215 type sequence W description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 12) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 13) chain A residue 219 type sequence G description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 14) chain A residue 226 type sequence G description BINDING SITE FOR RESIDUE 0ZJ A 299 source : AC1 15) chain D residue 57 type sequence H description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 16) chain D residue 60 type sequence L description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 17) chain D residue 99 type sequence L description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 18) chain D residue 189 type sequence D description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 19) chain D residue 190 type sequence A description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 20) chain D residue 193 type sequence G description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 21) chain D residue 194 type sequence D description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 22) chain D residue 195 type sequence S description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 23) chain D residue 214 type sequence S description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 24) chain D residue 215 type sequence W description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 25) chain D residue 216 type sequence G description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 26) chain D residue 219 type sequence G description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 27) chain D residue 226 type sequence G description BINDING SITE FOR RESIDUE 0ZJ D 299 source : AC2 28) chain F residue 106 type sequence D description BINDING SITE FOR RESIDUE HG F 998 source : AC3 29) chain C residue 106 type sequence D description BINDING SITE FOR RESIDUE HG C 999 source : AC4 30) chain F residue 106 type sequence D description BINDING SITE FOR RESIDUE HG F 997 source : AC5 31) chain C residue 106 type sequence D description BINDING SITE FOR RESIDUE HG C 996 source : AC6 32) chain F residue 84 type sequence Y description BINDING SITE FOR RESIDUE IMD F 2000 source : AC7 33) chain F residue 103 type sequence K description BINDING SITE FOR RESIDUE IMD F 2000 source : AC7 34) chain C residue 84 type sequence Y description BINDING SITE FOR RESIDUE IMD C 2001 source : AC8 35) chain C residue 103 type sequence K description BINDING SITE FOR RESIDUE IMD C 2001 source : AC8 36) chain F residue 247 type sequence Y description BINDING SITE FOR RESIDUE IMD F 2002 source : AC9 37) chain C residue 233 type sequence K description BINDING SITE FOR RESIDUE IMD C 2003 source : BC1 38) chain C residue 234 type sequence P description BINDING SITE FOR RESIDUE IMD C 2003 source : BC1 39) chain C residue 235 type sequence D description BINDING SITE FOR RESIDUE IMD C 2003 source : BC1 40) chain F residue 233 type sequence K description BINDING SITE FOR RESIDUE IMD F 2004 source : BC2 41) chain F residue 234 type sequence P description BINDING SITE FOR RESIDUE IMD F 2004 source : BC2 42) chain A residue 53-58 type prosite sequence LTAAHC description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC source prosite : PS00134 43) chain A residue 189-200 type prosite sequence DACEGDSGGPFV description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV source prosite : PS00135 44) chain A residue 57 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI1 45) chain A residue 102 type ACT_SITE sequence D description Charge relay system source Swiss-Prot : SWS_FT_FI1 46) chain A residue 195 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI1 47) chain D residue 57 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI1 48) chain D residue 102 type ACT_SITE sequence D description Charge relay system source Swiss-Prot : SWS_FT_FI1 49) chain D residue 195 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI1 50) chain A residue 15 type SITE sequence R description Cleavage; by factor Xa => ECO:0000269|PubMed:34265300 source Swiss-Prot : SWS_FT_FI2 51) chain D residue 15 type SITE sequence R description Cleavage; by factor Xa => ECO:0000269|PubMed:34265300 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 60 type CARBOHYD sequence L description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923 source Swiss-Prot : SWS_FT_FI3 53) chain D residue 60 type CARBOHYD sequence L description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923 source Swiss-Prot : SWS_FT_FI3

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