eF-site ID 1qjv-AB PDB Code 1qjv Chain A, B click to enlarge Title Pectin methylesterase PemA from Erwinia chrysanthemi Classification HYDROLASE (ASPARTYL ESTERASE) Compound PECTIN METHYLESTERASE Source (PMEA_ERWCH) Sequence A:  ATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIK NGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDG SKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDS DSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSG GRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKS GNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYG LGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWD KMSGKDKNGNTIWFNPEDSRFFEYKSYGAGAAVSKDRRQL TDAQAAEYTQSKVLGDWTPTLP B:  ATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIK NGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDG SKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDS DSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSG GRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKS GNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYG LGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWD KMSGKDKNGNTIWFNPEDSRFFEYKSYGAGAAVSKDRRQL TDAQAAEYTQSKVLGDWTPTLP Description (1)  PECTIN METHYLESTERASE (E.C.3.1.1.11) Functional site 1) chain A residue 272 type sequence T description BINDING SITE FOR RESIDUE CL A 400 source : AC1 2) chain B residue 272 type sequence T description BINDING SITE FOR RESIDUE CL B 400 source : AC2 3) chain A residue 194-203 type prosite sequence ISGTVDFIFG description PECTINESTERASE_2 Pectinesterase signature 2. IsGTVDFIFG source prosite : PS00503 4) chain A residue 178 type ACT_SITE sequence D description Proton donor source Swiss-Prot : SWS_FT_FI1 5) chain B residue 178 type ACT_SITE sequence D description Proton donor source Swiss-Prot : SWS_FT_FI1 6) chain A residue 199 type ACT_SITE sequence D description Nucleophile source Swiss-Prot : SWS_FT_FI2 7) chain B residue 199 type ACT_SITE sequence D description Nucleophile source Swiss-Prot : SWS_FT_FI2 8) chain A residue 109 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 9) chain B residue 153 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 10) chain B residue 219 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 11) chain B residue 226 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 12) chain B residue 230 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 267 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 14) chain B residue 269 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 272 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 153 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 219 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 226 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 230 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 267 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 269 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 272 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 109 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 177 type SITE sequence Q description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 177 type SITE sequence Q description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4

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