eF-site ID 2gc4-ABCDEFGH PDB Code 2gc4 Chain A, B, C, D, E, F, G, H 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 A:  EAETQAQETQGQAAARAAAADLAAGQDDEPRILEAPAPDA RRVYVNDPAHFAAVTQQFVIDGEAGRVIGMIDGGFLPNPV VADDGSFIAHASTVFSRIARGERTDYVEVFDPVTLLPTAD IELPDAPRFLVGTYPWMTSLTPDGKTLLFYQFSPAPAVGV VDLEGKAFKRMLDVPDCYHIFPTAPDTFFMHCRDGSLAKV AFGTEGTPEITHTEVFHPEDEFLINHPAYSQKAGRLVWPT YTGKIHQIDLSSGDAKFLPAVEALTEAERADGWRPGGWQQ VAYHRALDRIYLLVDQRDEWRHKTASRFVVVLDAKTGERL AKFEMGHEIDSINVSQDEKPLLYALSTGDKTLYIHDAESG EELRSVNQLGHGPQVITTADMG B:  TDPRAKWVPQDNDIQACDYWRHCSIDGNICDCSGGSLTNC PPGTKLATASXVASCYNPTDGQSYLIAYRDCCGYNVSGRC PCLNTEGELPVYRPEFANDIIWCFGAEDDAMTYHCTISPI VGKAS C:  DKATIPSESPFAAAEVADGAIVVDIAKMKYETPELHVKVG DTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSL TFTEAGTYDYHCTPHPFMRGKVVVE D:  APQFFNIIDGSPLNFDDAMEEGRDTEAVKHFLETGENVYN EDPEILPEAEELYAGMCSGCHGHYAEGKIGPGLNDAYWTY PGNETDVGLFSTLYGGATGQMGPMWGSLTLDEMLRTMAWV RHLYTGDPKDASWLTDEQKAGFTPFQP E:  EAETQAQETQGQAAARAAAADLAAGQDDEPRILEAPAPDA RRVYVNDPAHFAAVTQQFVIDGEAGRVIGMIDGGFLPNPV VADDGSFIAHASTVFSRIARGERTDYVEVFDPVTLLPTAD IELPDAPRFLVGTYPWMTSLTPDGKTLLFYQFSPAPAVGV VDLEGKAFKRMLDVPDCYHIFPTAPDTFFMHCRDGSLAKV AFGTEGTPEITHTEVFHPEDEFLINHPAYSQKAGRLVWPT YTGKIHQIDLSSGDAKFLPAVEALTEAERADGWRPGGWQQ VAYHRALDRIYLLVDQRDEWRHKTASRFVVVLDAKTGERL AKFEMGHEIDSINVSQDEKPLLYALSTGDKTLYIHDAESG EELRSVNQLGHGPQVITTADMG F:  TDPRAKWVPQDNDIQACDYWRHCSIDGNICDCSGGSLTNC PPGTKLATASXVASCYNPTDGQSYLIAYRDCCGYNVSGRC PCLNTEGELPVYRPEFANDIIWCFGAEDDAMTYHCTISPI VGKAS G:  DKATIPSESPFAAAEVADGAIVVDIAKMKYETPELHVKVG DTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSL TFTEAGTYDYHCTPHPFMRGKVVVE H:  APQFFNIIDGSPLNFDDAMEEGRDTEAVKHFLETGENVYN EDPEILPEAEELYAGMCSGCHGHYAEGKIGPGLNDAYWTY PGNETDVGLFSTLYGGATGQMGPMWGSLTLDEMLRTMAWV RHLYTGDPKDASWLTDEQKAGFTPFQP Description Functional site 1) chain G residue 53 type sequence H description BINDING SITE FOR RESIDUE CU G 107 source : AC1 2) chain G residue 92 type sequence C description BINDING SITE FOR RESIDUE CU G 107 source : AC1 3) chain G residue 95 type sequence H description BINDING SITE FOR RESIDUE CU G 107 source : AC1 4) chain G residue 98 type sequence M description BINDING SITE FOR RESIDUE CU G 107 source : AC1 5) chain C residue 53 type sequence H description BINDING SITE FOR RESIDUE CU C 107 source : AC4 6) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE CU C 107 source : AC4 7) chain C residue 95 type sequence H description BINDING SITE FOR RESIDUE CU C 107 source : AC4 8) chain C residue 98 type sequence M description BINDING SITE FOR RESIDUE CU C 107 source : AC4 9) chain G residue 31 type sequence E description BINDING SITE FOR RESIDUE NA H 603 source : AC7 10) chain H residue 72 type sequence G description BINDING SITE FOR RESIDUE NA H 603 source : AC7 11) chain H residue 75 type sequence D description BINDING SITE FOR RESIDUE NA H 603 source : AC7 12) chain H residue 77 type sequence Y description BINDING SITE FOR RESIDUE NA H 603 source : AC7 13) chain D residue 72 type sequence G description BINDING SITE FOR RESIDUE NA D 604 source : AC8 14) chain D residue 75 type sequence D description BINDING SITE FOR RESIDUE NA D 604 source : AC8 15) chain D residue 77 type sequence Y description BINDING SITE FOR RESIDUE NA D 604 source : AC8 16) chain H residue 56 type sequence M description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 17) chain H residue 57 type sequence C description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 18) chain H residue 60 type sequence C description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 19) chain H residue 61 type sequence H description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 20) chain H residue 71 type sequence P description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 21) chain H residue 73 type sequence L description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 22) chain H residue 78 type sequence W description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 23) chain H residue 79 type sequence T description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 24) chain H residue 80 type sequence Y description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 25) chain H residue 83 type sequence N description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 26) chain H residue 89 type sequence L description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 27) chain H residue 93 type sequence L description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 28) chain H residue 97 type sequence A description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 29) chain H residue 98 type sequence T description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 30) chain H residue 100 type sequence Q description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 31) chain H residue 101 type sequence M description BINDING SITE FOR RESIDUE HEC H 200 source : AC9 32) chain D residue 56 type sequence M description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 33) chain D residue 57 type sequence C description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 34) chain D residue 60 type sequence C description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 35) chain D residue 61 type sequence H description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 36) chain D residue 71 type sequence P description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 37) chain D residue 73 type sequence L description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 38) chain D residue 78 type sequence W description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 39) chain D residue 79 type sequence T description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 40) chain D residue 80 type sequence Y description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 41) chain D residue 83 type sequence N description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 42) chain D residue 89 type sequence L description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 43) chain D residue 93 type sequence L description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 44) chain D residue 97 type sequence A description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 45) chain D residue 98 type sequence T description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 46) chain D residue 100 type sequence Q description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 47) chain D residue 101 type sequence M description BINDING SITE FOR RESIDUE HEC D 200 source : BC2 48) chain C residue 85-98 type prosite sequence AGTYDYHCTPHPFM description COPPER_BLUE Type-1 copper (blue) proteins signature. AgtYdYHCt.P.Hpf..M source prosite : PS00196 49) chain B residue 32 type catalytic sequence D description 13 source MCSA : MCSA1 50) chain B residue 57 type catalytic sequence X description 13 source MCSA : MCSA1 51) chain B residue 76 type catalytic sequence D description 13 source MCSA : MCSA1 52) chain B residue 108 type catalytic sequence W description 13 source MCSA : MCSA1 53) chain B residue 119 type catalytic sequence Y description 13 source MCSA : MCSA1 54) chain B residue 122 type catalytic sequence T description 13 source MCSA : MCSA1 55) chain F residue 32 type catalytic sequence D description 13 source MCSA : MCSA2 56) chain F residue 57 type catalytic sequence X description 13 source MCSA : MCSA2 57) chain F residue 76 type catalytic sequence D description 13 source MCSA : MCSA2 58) chain F residue 108 type catalytic sequence W description 13 source MCSA : MCSA2 59) chain F residue 119 type catalytic sequence Y description 13 source MCSA : MCSA2 60) chain F residue 122 type catalytic sequence T description 13 source MCSA : MCSA2 61) chain D residue 57 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 62) chain D residue 60 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 63) chain H residue 57 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 64) chain H residue 60 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 65) chain H residue 61 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 66) chain D residue 61 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2

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