eF-site ID 1agm-A PDB Code 1agm Chain A click to enlarge Title Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution Classification HYDROLASE Compound GLUCOAMYLASE-471 Source Aspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi) (AMYG_ASPAK) Sequence A:  ATLDSWLSNEATVARTAILNNIGADGAWVSGADSGIVVAS PSTDNPDYFYTWTRDSGLVIKTLVDLFRNGDTDLLSTIEH YISSQAIIQGVSNPSGDLSSGGLGEPKFNVDETAYTGSWG RPQRDGPALRATAMIGFGQWLLDNGYTSAATEIVWPLVRN DLSYVAQYWNQTGYDLWEEVNGSSFFTIAVQHRALVEGSA FATAVGSSCSWCDSQAPQILCYLQSFWTGSYILANFDSSR SGKDTNTLLGSIHTFDPEAGCDDSTFQPCSPRALANHKEV VDSFRSIYTLNDGLSDSEAVAVGRYPEDSYYNGNPWFLCT LAAAEQLYDALYQWDKQGSLEITDVSLDFFKALYSGAATG TYSSSSSTYSSIVSAVKTFADGFVSIVETHAASNGSLSEQ FDKSDGDELSARDLTWSYAALLTANNRRNSVVPPSWGETS ASSVPGTCAATSASGTYSSVTVTSWPSIVA Description (1)  GLUCOAMYLASE-471 (GLUCAN 1,4-ALPHA-GLUCOSIDASE, RESIDUES 1 - 471) (E.C.3.2.1.3) COMPLEXED WITH ACARBOSE Functional site 1) chain A residue 54 type sequence R description SUBSITE 1 OF THE ACTIVE SITE source : SB1 2) chain A residue 55 type sequence D description SUBSITE 1 OF THE ACTIVE SITE source : SB1 3) chain A residue 177 type sequence L description SUBSITE 1 OF THE ACTIVE SITE source : SB1 4) chain A residue 179 type sequence E description SUBSITE 1 OF THE ACTIVE SITE source : SB1 5) chain A residue 305 type sequence R description SUBSITE 1 OF THE ACTIVE SITE source : SB1 6) chain A residue 400 type sequence E description SUBSITE 1 OF THE ACTIVE SITE source : SB1 7) chain A residue 176 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10051 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 179 type ACT_SITE sequence E description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10051 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 120 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 121 type catalytic sequence G description 393 source MCSA : MCSA1 11) chain A residue 177 type catalytic sequence L description 393 source MCSA : MCSA1 12) chain A residue 180 type catalytic sequence E description 393 source MCSA : MCSA1 13) chain A residue 181 type catalytic sequence V description 393 source MCSA : MCSA1 14) chain A residue 401 type catalytic sequence Q description 393 source MCSA : MCSA1 15) chain A residue 180 type ACT_SITE sequence E description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10051, ECO:0000269|PubMed:1970434 source Swiss-Prot : SWS_FT_FI10 16) chain A residue 172 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI12 17) chain A residue 396 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI12 18) chain A residue 452 type CARBOHYD sequence T description O-linked (Man) threonine => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 19) chain A residue 462 type CARBOHYD sequence T description O-linked (Man) threonine => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 20) chain A residue 464 type CARBOHYD sequence T description O-linked (Man) threonine => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 21) chain A residue 453 type CARBOHYD sequence S description O-linked (Man) threonine source Swiss-Prot : SWS_FT_FI8 22) chain A residue 463 type CARBOHYD sequence V description O-linked (Man) threonine source Swiss-Prot : SWS_FT_FI8 23) chain A residue 465 type CARBOHYD sequence S description O-linked (Man) threonine source Swiss-Prot : SWS_FT_FI8 24) chain A residue 121 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI11 25) chain A residue 177 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10051, ECO:0000269|PubMed:1970434 source Swiss-Prot : SWS_FT_FI9 26) chain A residue 171 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 395 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 441 type CARBOHYD sequence S description O-linked (Man) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 443 type CARBOHYD sequence S description O-linked (Man) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 459 type CARBOHYD sequence S description O-linked (Man) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 468 type CARBOHYD sequence S description O-linked (Man) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 442 type CARBOHYD sequence A description O-linked (Man) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 469 type CARBOHYD sequence I description O-linked (Man) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 444 type CARBOHYD sequence S description O-linked (Man) serine source Swiss-Prot : SWS_FT_FI6 35) chain A residue 460 type CARBOHYD sequence S description O-linked (Man) serine source Swiss-Prot : SWS_FT_FI6 36) chain A residue 445 type CARBOHYD sequence V description O-linked (Man) serine source Swiss-Prot : SWS_FT_FI6 37) chain A residue 454 type CARBOHYD sequence A description O-linked (Man) serine source Swiss-Prot : SWS_FT_FI6 38) chain A residue 461 type CARBOHYD sequence V description O-linked (Man) serine source Swiss-Prot : SWS_FT_FI6 39) chain A residue 403-415 type prosite sequence DKSDGDELSARDL description EF_HAND_1 EF-hand calcium-binding domain. DKSDGDELSarDL source prosite : PS00018 40) chain A residue 173-183 type prosite sequence TGYDLWEEVNG description GLUCOAMYLASE Glucoamylase active site region signature. TGy.DlWEEvnG source prosite : PS00820

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