eF-site ID 2gc4-IJKLMNOP PDB Code 2gc4 Chain I, J, K, L, M, N, O, P click to enlarge Title Structural comparison of the oxidized ternary electron transfer complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans with the substrate-reduced, copper free complex at 1.9 A resolution. Classification Oxidoreductase, Electron transport Compound Methylamine dehydrogenase heavy chain Source ORGANISM_SCIENTIFIC: Paracoccus denitrificans; Sequence I:  EAETQAQETQGQAAARAAAADLAAGQDDEPRILEAPAPDA RRVYVNDPAHFAAVTQQFVIDGEAGRVIGMIDGGFLPNPV VADDGSFIAHASTVFSRIARGERTDYVEVFDPVTLLPTAD IELPDAPRFLVGTYPWMTSLTPDGKTLLFYQFSPAPAVGV VDLEGKAFKRMLDVPDCYHIFPTAPDTFFMHCRDGSLAKV AFGTEGTPEITHTEVFHPEDEFLINHPAYSQKAGRLVWPT YTGKIHQIDLSSGDAKFLPAVEALTEAERADGWRPGGWQQ VAYHRALDRIYLLVDQRDEWRHKTASRFVVVLDAKTGERL AKFEMGHEIDSINVSQDEKPLLYALSTGDKTLYIHDAESG EELRSVNQLGHGPQVITTADMG J:  TDPRAKWVPQDNDIQACDYWRHCSIDGNICDCSGGSLTNC PPGTKLATASXVASCYNPTDGQSYLIAYRDCCGYNVSGRC PCLNTEGELPVYRPEFANDIIWCFGAEDDAMTYHCTISPI VGKAS K:  DKATIPSESPFAAAEVADGAIVVDIAKMKYETPELHVKVG DTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSL TFTEAGTYDYHCTPHPFMRGKVVVE L:  APQFFNIIDGSPLNFDDAMEEGRDTEAVKHFLETGENVYN EDPEILPEAEELYAGMCSGCHGHYAEGKIGPGLNDAYWTY PGNETDVGLFSTLYGGATGQMGPMWGSLTLDEMLRTMAWV RHLYTGDPKDASWLTDEQKAGFTPFQP M:  EAETQAQETQGQAAARAAAADLAAGQDDEPRILEAPAPDA RRVYVNDPAHFAAVTQQFVIDGEAGRVIGMIDGGFLPNPV VADDGSFIAHASTVFSRIARGERTDYVEVFDPVTLLPTAD IELPDAPRFLVGTYPWMTSLTPDGKTLLFYQFSPAPAVGV VDLEGKAFKRMLDVPDCYHIFPTAPDTFFMHCRDGSLAKV AFGTEGTPEITHTEVFHPEDEFLINHPAYSQKAGRLVWPT YTGKIHQIDLSSGDAKFLPAVEALTEAERADGWRPGGWQQ VAYHRALDRIYLLVDQRDEWRHKTASRFVVVLDAKTGERL AKFEMGHEIDSINVSQDEKPLLYALSTGDKTLYIHDAESG EELRSVNQLGHGPQVITTADMG N:  TDPRAKWVPQDNDIQACDYWRHCSIDGNICDCSGGSLTNC PPGTKLATASXVASCYNPTDGQSYLIAYRDCCGYNVSGRC PCLNTEGELPVYRPEFANDIIWCFGAEDDAMTYHCTISPI VGKAS O:  DKATIPSESPFAAAEVADGAIVVDIAKMKYETPELHVKVG DTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSL TFTEAGTYDYHCTPHPFMRGKVVVE P:  APQFFNIIDGSPLNFDDAMEEGRDTEAVKHFLETGENVYN EDPEILPEAEELYAGMCSGCHGHYAEGKIGPGLNDAYWTY PGNETDVGLFSTLYGGATGQMGPMWGSLTLDEMLRTMAWV RHLYTGDPKDASWLTDEQKAGFTPFQP Description Functional site 1) chain K residue 53 type sequence H description BINDING SITE FOR RESIDUE CU K 107 source : AC2 2) chain K residue 92 type sequence C description BINDING SITE FOR RESIDUE CU K 107 source : AC2 3) chain K residue 95 type sequence H description BINDING SITE FOR RESIDUE CU K 107 source : AC2 4) chain K residue 98 type sequence M description BINDING SITE FOR RESIDUE CU K 107 source : AC2 5) chain O residue 53 type sequence H description BINDING SITE FOR RESIDUE CU O 107 source : AC3 6) chain O residue 92 type sequence C description BINDING SITE FOR RESIDUE CU O 107 source : AC3 7) chain O residue 95 type sequence H description BINDING SITE FOR RESIDUE CU O 107 source : AC3 8) chain O residue 98 type sequence M description BINDING SITE FOR RESIDUE CU O 107 source : AC3 9) chain K residue 31 type sequence E description BINDING SITE FOR RESIDUE NA L 601 source : AC5 10) chain L residue 72 type sequence G description BINDING SITE FOR RESIDUE NA L 601 source : AC5 11) chain L residue 75 type sequence D description BINDING SITE FOR RESIDUE NA L 601 source : AC5 12) chain L residue 77 type sequence Y description BINDING SITE FOR RESIDUE NA L 601 source : AC5 13) chain O residue 31 type sequence E description BINDING SITE FOR RESIDUE NA P 602 source : AC6 14) chain P residue 72 type sequence G description BINDING SITE FOR RESIDUE NA P 602 source : AC6 15) chain P residue 75 type sequence D description BINDING SITE FOR RESIDUE NA P 602 source : AC6 16) chain P residue 77 type sequence Y description BINDING SITE FOR RESIDUE NA P 602 source : AC6 17) chain L residue 56 type sequence M description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 18) chain L residue 57 type sequence C description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 19) chain L residue 60 type sequence C description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 20) chain L residue 61 type sequence H description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 21) chain L residue 71 type sequence P description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 22) chain L residue 73 type sequence L description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 23) chain L residue 78 type sequence W description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 24) chain L residue 79 type sequence T description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 25) chain L residue 80 type sequence Y description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 26) chain L residue 83 type sequence N description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 27) chain L residue 89 type sequence L description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 28) chain L residue 97 type sequence A description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 29) chain L residue 98 type sequence T description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 30) chain L residue 100 type sequence Q description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 31) chain L residue 101 type sequence M description BINDING SITE FOR RESIDUE HEC L 200 source : BC1 32) chain P residue 56 type sequence M description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 33) chain P residue 57 type sequence C description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 34) chain P residue 60 type sequence C description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 35) chain P residue 61 type sequence H description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 36) chain P residue 71 type sequence P description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 37) chain P residue 73 type sequence L description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 38) chain P residue 78 type sequence W description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 39) chain P residue 79 type sequence T description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 40) chain P residue 80 type sequence Y description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 41) chain P residue 83 type sequence N description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 42) chain P residue 93 type sequence L description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 43) chain P residue 97 type sequence A description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 44) chain P residue 98 type sequence T description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 45) chain P residue 100 type sequence Q description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 46) chain P residue 101 type sequence M description BINDING SITE FOR RESIDUE HEC P 200 source : BC3 47) chain J residue 32 type catalytic sequence D description 13 source MCSA : MCSA3 48) chain J residue 57 type catalytic sequence X description 13 source MCSA : MCSA3 49) chain J residue 76 type catalytic sequence D description 13 source MCSA : MCSA3 50) chain J residue 108 type catalytic sequence W description 13 source MCSA : MCSA3 51) chain J residue 119 type catalytic sequence Y description 13 source MCSA : MCSA3 52) chain J residue 122 type catalytic sequence T description 13 source MCSA : MCSA3 53) chain N residue 32 type catalytic sequence D description 13 source MCSA : MCSA4 54) chain N residue 57 type catalytic sequence X description 13 source MCSA : MCSA4 55) chain N residue 76 type catalytic sequence D description 13 source MCSA : MCSA4 56) chain N residue 108 type catalytic sequence W description 13 source MCSA : MCSA4 57) chain N residue 119 type catalytic sequence Y description 13 source MCSA : MCSA4 58) chain N residue 122 type catalytic sequence T description 13 source MCSA : MCSA4 59) chain K residue 92 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 60) chain K residue 95 type BINDING sequence H description covalent source Swiss-Prot : SWS_FT_FI1 61) chain K residue 98 type BINDING sequence M description covalent source Swiss-Prot : SWS_FT_FI1 62) chain O residue 53 type BINDING sequence H description covalent source Swiss-Prot : SWS_FT_FI1 63) chain O residue 92 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 64) chain O residue 95 type BINDING sequence H description covalent source Swiss-Prot : SWS_FT_FI1 65) chain O residue 98 type BINDING sequence M description covalent source Swiss-Prot : SWS_FT_FI1 66) chain L residue 57 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 67) chain L residue 60 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 68) chain P residue 57 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 69) chain P residue 60 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 70) chain K residue 53 type BINDING sequence H description covalent source Swiss-Prot : SWS_FT_FI1 71) chain L residue 61 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 72) chain P residue 61 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 73) chain J residue 57 type BINDING sequence X description axial binding residue source Swiss-Prot : SWS_FT_FI2 74) chain J residue 108 type BINDING sequence W description axial binding residue source Swiss-Prot : SWS_FT_FI2 75) chain N residue 57 type BINDING sequence X description axial binding residue source Swiss-Prot : SWS_FT_FI2 76) chain N residue 108 type BINDING sequence W description axial binding residue source Swiss-Prot : SWS_FT_FI2

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