eF-site ID 5edm-A PDB Code 5edm Chain A click to enlarge Title Crystal structure of prothrombin deletion mutant residues 154-167 ( Form I ) Classification HYDROLASE Compound Prothrombin Source (THRB_HUMAN) Sequence A:  ANTFLXXVRKGNLXRXCVXXTCSYXXAFXALXSSTATDVF WAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNIT RSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSS TMGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTEQCVPDR GQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQL VENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEE ETSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTEREL LESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASL ISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYE RNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFS DYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANV GKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKP DEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCD RDGKYGFYTHVFRLKKWIQKVIDQFGEYLE Description Functional site 1) chain A residue 113-126 type prosite sequence FCRNPDSSTMGPWC description KRINGLE_1 Kringle domain signature. FCRNpdsstmgpWC source prosite : PS00021 2) chain A residue 204-217 type prosite sequence FCRNPDGDEEGVWC description KRINGLE_1 Kringle domain signature. FCRNpdsstmgpWC source prosite : PS00021 3) chain A residue 78 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320 source Swiss-Prot : SWS_FT_FI6 4) chain A residue 100 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320 source Swiss-Prot : SWS_FT_FI6 5) chain A residue 373 type CARBOHYD sequence S 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_FI7 6) chain A residue 14 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI5 7) chain A residue 16 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI5 8) chain A residue 19 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI5 9) chain A residue 20 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI5 10) chain A residue 25 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI5 11) chain A residue 26 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI5 12) chain A residue 29 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI5 13) chain A residue 32 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI5 14) chain A residue 16-41 type prosite sequence XCVXXTCSYXXAFXALXSSTATDVFW description GLA_1 Vitamin K-dependent carboxylation domain. EcvEEtCsyeeafEalesstatdv.FW source prosite : PS00011 15) chain A residue 345-350 type prosite sequence LTAAHC description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC source prosite : PS00134 16) chain A residue 505-516 type prosite sequence DACEGDSGGPFV description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV source prosite : PS00135 17) chain A residue 271 type SITE sequence T description Cleavage; by factor Xa => ECO:0000269|PubMed:34265300 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 320 type SITE sequence W description Cleavage; by factor Xa => ECO:0000269|PubMed:34265300 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 363 type ACT_SITE sequence N description Charge relay system source Swiss-Prot : SWS_FT_FI1 20) chain A residue 419 type ACT_SITE sequence D description Charge relay system source Swiss-Prot : SWS_FT_FI1 21) chain A residue 525 type ACT_SITE sequence W description Charge relay system source Swiss-Prot : SWS_FT_FI1 22) chain A residue 155 type SITE sequence Q description Cleavage; by thrombin source Swiss-Prot : SWS_FT_FI2 23) chain A residue 6 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 7 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407 source Swiss-Prot : SWS_FT_FI4

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