eF-site ID 1cfm-ABC PDB Code 1cfm Chain A, B, C click to enlarge Title CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII Classification ELECTRON TRANSPORT Compound CYTOCHROME F Source ORGANISM_SCIENTIFIC: Chlamydomonas reinhardtii; Sequence A:  YPVFAQQNYANPREANGRIVCANCHLAQKAVEIEVPQAVL PDTVFEAVIELPYDKQVKQVLANGKKGDLNVGMVLILPEG FELAPPDRVPAEIKEKVGNLYYQPYSPEQKNILVVGPVPG KKYSEMVVPILSPDPAKNKNVSYLKYPIYFGGNRGRGQVY PDGKKSNNTIYNASAAGKIVAITALSEKKGGFEVSIEKAN GEVVVDKIPAGPDLIVKEGQTVQADQPLTNNPNVGGFGQA ETEIVLQNPAR B:  YPVFAQQNYANPREANGRIVCANCHLAQKAVEIEVPQAVL PDTVFEAVIELPYDKQVKQVLANGKKGDLNVGMVLILPEG FELAPPDRVPAEIKEKVGNLYYQPYSPEQKNILVVGPVPG KKYSEMVVPILSPDPAKNKNVSYLKYPIYFGGNRGRGQVY PDGKKSNNTIYNASAAGKIVAITALSEKKGGFEVSIEKAN GEVVVDKIPAGPDLIVKEGQTVQADQPLTNNPNVGGFGQA ETEIVLQNPAR C:  YPVFAQQNYANPREANGRIVCANCHLAQKAVEIEVPQAVL PDTVFEAVIELPYDKQVKQVLANGKKGDLNVGMVLILPEG FELAPPDRVPAEIKEKVGNLYYQPYSPEQKNILVVGPVPG KKYSEMVVPILSPDPAKNKNVSYLKYPIYFGGNRGRGQVY PDGKKSNNTIYNASAAGKIVAITALSEKKGGFEVSIEKAN GEVVVDKIPAGPDLIVKEGQTVQADQPLTNNPNVGGFGQA ETEIVLQNPAR Description Functional site 1) chain A residue 1 type sequence Y description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 2) chain A residue 4 type sequence F description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 3) chain A residue 5 type sequence A description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 4) chain A residue 9 type sequence Y description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 5) chain A residue 21 type sequence C description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 6) chain A residue 24 type sequence C description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 7) chain A residue 25 type sequence H description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 8) chain A residue 59 type sequence Q description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 9) chain A residue 69 type sequence L description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 10) chain A residue 70 type sequence N description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 11) chain A residue 71 type sequence V description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 12) chain A residue 72 type sequence G description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 13) chain A residue 73 type sequence M description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 14) chain A residue 153 type sequence N description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 15) chain A residue 155 type sequence G description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 16) chain A residue 156 type sequence R description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 17) chain A residue 157 type sequence G description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 18) chain A residue 159 type sequence V description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 19) chain A residue 160 type sequence Y description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 20) chain A residue 161 type sequence P description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 21) chain C residue 16 type sequence N description BINDING SITE FOR RESIDUE HEM A 253 source : AC1 22) chain B residue 1 type sequence Y description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 23) chain B residue 2 type sequence P description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 24) chain B residue 4 type sequence F description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 25) chain B residue 5 type sequence A description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 26) chain B residue 9 type sequence Y description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 27) chain B residue 20 type sequence V description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 28) chain B residue 21 type sequence C description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 29) chain B residue 24 type sequence C description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 30) chain B residue 25 type sequence H description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 31) chain B residue 59 type sequence Q description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 32) chain B residue 69 type sequence L description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 33) chain B residue 70 type sequence N description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 34) chain B residue 71 type sequence V description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 35) chain B residue 72 type sequence G description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 36) chain B residue 73 type sequence M description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 37) chain B residue 153 type sequence N description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 38) chain B residue 155 type sequence G description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 39) chain B residue 156 type sequence R description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 40) chain B residue 157 type sequence G description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 41) chain B residue 159 type sequence V description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 42) chain B residue 160 type sequence Y description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 43) chain B residue 161 type sequence P description BINDING SITE FOR RESIDUE HEM B 254 source : AC2 44) chain C residue 1 type sequence Y description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 45) chain C residue 2 type sequence P description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 46) chain C residue 4 type sequence F description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 47) chain C residue 5 type sequence A description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 48) chain C residue 21 type sequence C description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 49) chain C residue 24 type sequence C description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 50) chain C residue 25 type sequence H description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 51) chain C residue 59 type sequence Q description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 52) chain C residue 69 type sequence L description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 53) chain C residue 70 type sequence N description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 54) chain C residue 71 type sequence V description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 55) chain C residue 72 type sequence G description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 56) chain C residue 73 type sequence M description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 57) chain C residue 74 type sequence V description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 58) chain C residue 153 type sequence N description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 59) chain C residue 155 type sequence G description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 60) chain C residue 156 type sequence R description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 61) chain C residue 157 type sequence G description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 62) chain C residue 159 type sequence V description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 63) chain C residue 160 type sequence Y description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 64) chain C residue 161 type sequence P description BINDING SITE FOR RESIDUE HEM C 255 source : AC3 65) chain A residue 1 type BINDING sequence Y description axial binding residue => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI1 66) chain A residue 25 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI1 67) chain B residue 1 type BINDING sequence Y description axial binding residue => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 25 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI1 69) chain C residue 1 type BINDING sequence Y description axial binding residue => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI1 70) chain C residue 25 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI1 71) chain A residue 21 type BINDING sequence C description covalent => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI2 72) chain A residue 24 type BINDING sequence C description covalent => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI2 73) chain B residue 21 type BINDING sequence C description covalent => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI2 74) chain B residue 24 type BINDING sequence C description covalent => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI2 75) chain C residue 21 type BINDING sequence C description covalent => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI2 76) chain C residue 24 type BINDING sequence C description covalent => ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110 source Swiss-Prot : SWS_FT_FI2

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