eF-site ID 1a4w-HIL PDB Code 1a4w Chain H, I, L click to enlarge Title CRYSTAL STRUCTURES OF THROMBIN WITH THIAZOLE-CONTAINING INHIBITORS: PROBES OF THE S1' BINDING SITE Classification HYDROLASE/HYDROLASE INHIBITOR Compound ALPHA-THROMBIN (SMALL SUBUNIT) Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence H:  IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLT AAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCL PDRETAASLLQAGYKGRVTGWGNLKEGQPSVLQVVNLPIV ERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGP FVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKK WIQKVIDQ I:  DFEEIPEEX L:  DCGLRPLFEKKSLEDKTERELLESYI Description Functional site 1) chain H residue 57 type sequence H description ACTIVE SITE source : CAT 2) chain H residue 102 type sequence D description ACTIVE SITE source : CAT 3) chain H residue 195 type sequence S description ACTIVE SITE source : CAT 4) chain H residue 221 type sequence D description BINDING SITE FOR RESIDUE NA H 541 source : AC1 5) chain H residue 224 type sequence K description BINDING SITE FOR RESIDUE NA H 541 source : AC1 6) chain H residue 169 type sequence K description BINDING SITE FOR RESIDUE NA H 542 source : AC2 7) chain H residue 172 type sequence T description BINDING SITE FOR RESIDUE NA H 542 source : AC2 8) chain H residue 204 type sequence P description BINDING SITE FOR RESIDUE NA H 542 source : AC2 9) chain H residue 57 type sequence H description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 10) chain H residue 60 type sequence L description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 11) chain H residue 60 type sequence L description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 12) chain H residue 60 type sequence L description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 13) chain H residue 97 type sequence R description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 14) chain H residue 99 type sequence L description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 15) chain H residue 189 type sequence D description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 16) chain H residue 190 type sequence A description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 17) chain H residue 215 type sequence W description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 18) chain H residue 216 type sequence G description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 19) chain H residue 219 type sequence G description BINDING SITE FOR RESIDUE QWE H 373 source : AC3 20) chain H residue 34 type sequence F description BINDING SITE FOR CHAIN I OF HIRUGEN source : AC4 21) chain H residue 67 type sequence R description BINDING SITE FOR CHAIN I OF HIRUGEN source : AC4 22) chain H residue 73 type sequence R description BINDING SITE FOR CHAIN I OF HIRUGEN source : AC4 23) chain H residue 74 type sequence T description BINDING SITE FOR CHAIN I OF HIRUGEN source : AC4 24) chain H residue 75 type sequence R description BINDING SITE FOR CHAIN I OF HIRUGEN source : AC4 25) chain H residue 76 type sequence Y description BINDING SITE FOR CHAIN I OF HIRUGEN source : AC4 26) chain H residue 81 type sequence K description BINDING SITE FOR CHAIN I OF HIRUGEN source : AC4 27) chain H residue 82 type sequence I description BINDING SITE FOR CHAIN I OF HIRUGEN source : AC4 28) chain H residue 53-58 type prosite sequence LTAAHC description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC source prosite : PS00134 29) chain H residue 189-200 type prosite sequence DACEGDSGGPFV description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV source prosite : PS00135 30) chain I residue 363 type MOD_RES sequence X description Sulfotyrosine => ECO:0000269|PubMed:3513162 source Swiss-Prot : SWS_FT_FI1 31) chain H residue 102 type MOD_RES sequence D description Sulfotyrosine => ECO:0000269|PubMed:3513162 source Swiss-Prot : SWS_FT_FI1 32) chain H residue 195 type MOD_RES sequence S description Sulfotyrosine => ECO:0000269|PubMed:3513162 source Swiss-Prot : SWS_FT_FI1 33) chain H 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_FI2

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