eF-site ID 1chi-A PDB Code 1chi Chain A click to enlarge Title STRUCTURAL STUDIES OF THE ROLES OF RESIDUES 82 AND 85 AT THE INTERACTIVE FACE OF CYTOCHROME C Classification ELECTRON TRANSPORT(HEME PROTEIN) Compound CYTOCHROME C Source null (CYC1_YEAST) Sequence A:  TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGI FGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPXKYI PGTKMAYGGAKKEKDRNDLITYLKKATE Description (1)  CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH PHE 82 REPLACED BY TYR, LEU 85 REPLACED BY ALA, AND CYS 102 REPLACED BY THR (F82Y,L85A,C102T) Functional site 1) chain A residue 2 type sequence S description BINDING SITE FOR RESIDUE SO4 A 117 source : AC1 2) chain A residue 3 type sequence A description BINDING SITE FOR RESIDUE SO4 A 117 source : AC1 3) chain A residue 4 type sequence K description BINDING SITE FOR RESIDUE SO4 A 117 source : AC1 4) chain A residue 47 type sequence S description BINDING SITE FOR RESIDUE SO4 A 117 source : AC1 5) chain A residue 73 type sequence K description BINDING SITE FOR RESIDUE SO4 A 117 source : AC1 6) chain A residue 13 type sequence R description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 7) chain A residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 8) chain A residue 16 type sequence Q description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 9) chain A residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 10) chain A residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 11) chain A residue 23 type sequence G description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 12) chain A residue 28 type sequence V description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 13) chain A residue 35 type sequence I description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 14) chain A residue 40 type sequence S description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 15) chain A residue 41 type sequence G description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 16) chain A residue 46 type sequence Y description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 17) chain A residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 18) chain A residue 49 type sequence T description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 19) chain A residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 20) chain A residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 21) chain A residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 22) chain A residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 23) chain A residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 24) chain A residue 82 type sequence Y description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 25) chain A residue 94 type sequence L description BINDING SITE FOR RESIDUE HEC A 104 source : AC2 26) chain A residue 74 type MOD_RES sequence Y description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 15 type BINDING sequence L description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 18 type BINDING sequence H description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 19 type BINDING sequence T description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 81 type BINDING sequence A description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 73 type MOD_RES sequence K description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3

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