eF-site ID 8kme-2 PDB Code 8kme Chain 2 click to enlarge Title CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN INHIBITED WITH SEL2770. Classification HYDROLASE/HYDROLASE INHIBITOR Compound THROMBIN Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence 2:  IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLT AAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCL PDRETAASLLQAGYKGRVTGWGNLKETGQPSVLQVVNLPI VERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGG PFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLK KWIQKVIDQF Description Functional site 1) chain 2 residue 169 type sequence K description BINDING SITE FOR RESIDUE NA 2 950 source : AC1 2) chain 2 residue 172 type sequence T description BINDING SITE FOR RESIDUE NA 2 950 source : AC1 3) chain 2 residue 224 type sequence K description BINDING SITE FOR RESIDUE NA 2 951 source : AC2 4) chain 2 residue 34 type sequence F description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 5) chain 2 residue 36 type sequence K description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 6) chain 2 residue 38 type sequence Q description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 7) chain 2 residue 65 type sequence L description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 8) chain 2 residue 73 type sequence R description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 9) chain 2 residue 74 type sequence T description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 10) chain 2 residue 76 type sequence Y description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 11) chain 2 residue 80 type sequence E description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 12) chain 2 residue 81 type sequence K description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 13) chain 2 residue 82 type sequence I description BINDING SITE FOR CHAIN 3 OF N-ACETYLHIRUDIN source : AC3 14) chain 2 residue 99 type sequence L description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 15) chain 2 residue 174 type sequence I description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 16) chain 2 residue 189 type sequence D description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 17) chain 2 residue 190 type sequence A description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 18) chain 2 residue 192 type sequence E description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 19) chain 2 residue 214 type sequence S description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 20) chain 2 residue 215 type sequence W description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 21) chain 2 residue 216 type sequence G description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 22) chain 2 residue 217 type sequence E description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 23) chain 2 residue 219 type sequence G description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 24) chain 2 residue 220 type sequence C description BINDING SITE FOR CHAIN 4 OF SEL2770 source : AC4 25) chain 2 residue 57 type sequence H description CATALYTIC SITE source : CAT 26) chain 2 residue 102 type sequence D description CATALYTIC SITE source : CAT 27) chain 2 residue 195 type sequence S description CATALYTIC SITE source : CAT 28) chain 2 residue 57 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI1 29) chain 2 residue 102 type ACT_SITE sequence D description Charge relay system source Swiss-Prot : SWS_FT_FI1 30) chain 2 residue 195 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI1 31) chain 2 residue 53-58 type prosite sequence LTAAHC description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC source prosite : PS00134 32) chain 2 residue 189-200 type prosite sequence DACEGDSGGPFV description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV source prosite : PS00135 33) chain 2 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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