eF-site ID 2jk4-A PDB Code 2jk4 Chain A click to enlarge Title Structure of the human voltage-dependent anion channel Classification TRANSPORT Compound VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL PROTEIN 1 Source (VDAC1_HUMAN) Sequence A:  MRGSAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSEN GLEFTSSGSANTETTKVTGSLETKYRWTEYGLTFTEKWNT DNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTG YKREHINLGCDMDFDIAGPSIRGALVLGYEGWLAGYQMNF ETAKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQK VNKKLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKV NNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGL GLEFQARS Description (1)  VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL PROTEIN 1 Functional site 1) chain A residue 269 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI14 2) chain A residue 15 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:32047033 source Swiss-Prot : SWS_FT_FI15 3) chain A residue 56 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:32047033 source Swiss-Prot : SWS_FT_FI16 4) chain A residue 113 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:32047033 source Swiss-Prot : SWS_FT_FI16 5) chain A residue 277 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:32047033 source Swiss-Prot : SWS_FT_FI16 6) chain A residue 23 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:32047033 source Swiss-Prot : SWS_FT_FI17 7) chain A residue 64 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951 source Swiss-Prot : SWS_FT_FI18 8) chain A residue 164 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951 source Swiss-Prot : SWS_FT_FI18 9) chain A residue 112 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:32047033 source Swiss-Prot : SWS_FT_FI19 10) chain A residue 269 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:25621951 source Swiss-Prot : SWS_FT_FI20 11) chain A residue 29-38 type TRANSMEM sequence LIKLDLKTKS description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 153-161 type TRANSMEM sequence LAGYQMNFE description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 166-178 type TRANSMEM sequence RVTQSNFAVGYKT description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 181-188 type TRANSMEM sequence FQLHTNVN description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 192-201 type TRANSMEM sequence EFGGSIYQKV description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 205-214 type TRANSMEM sequence LETAVNLAWT description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 221-230 type TRANSMEM sequence RFGIAAKYQI description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 234-241 type TRANSMEM sequence ACFSAKVN description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 245-254 type TRANSMEM sequence LIGLGYTQTL description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 257-266 type TRANSMEM sequence GIKLTLSALL description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 276-285 type TRANSMEM sequence HKLGLGLEFQ description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 42-50 type TRANSMEM sequence LEFTSSGSA description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 57-67 type TRANSMEM sequence VTGSLETKYRW description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 72-79 type TRANSMEM sequence LTFTEKWN description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 83-92 type TRANSMEM sequence TLGTEITVED description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 98-107 type TRANSMEM sequence LKLTFDSSFS description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 114-123 type TRANSMEM sequence NAKIKTGYKR description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 126-133 type TRANSMEM sequence INLGCDMD description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 140-148 type TRANSMEM sequence SIRGALVLG description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 112 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q60932 source Swiss-Prot : SWS_FT_FI10 31) chain A residue 196 type MOD_RES sequence S description Phosphoserine; by NEK1 => ECO:0000269|PubMed:20230784 source Swiss-Prot : SWS_FT_FI11 32) chain A residue 243 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI12 33) chain A residue 245 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18755977 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 263 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18755977 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 255 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q60932 source Swiss-Prot : SWS_FT_FI13 36) chain A residue 76 type SITE sequence E description Involved in ceramide and phosphatidylcholine binding. Critical for channel structural stability and gating => ECO:0000269|PubMed:31015432, ECO:0000305|PubMed:18832158 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 5 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|PubMed:2559745, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 16 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9Z2L0 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 22 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q60932 source Swiss-Prot : SWS_FT_FI6 40) chain A residue 23 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q60932 source Swiss-Prot : SWS_FT_FI7 41) chain A residue 70 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q60932 source Swiss-Prot : SWS_FT_FI8 42) chain A residue 110 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 43) chain A residue 228-250 type prosite sequence YQIDPDACFSAKVNNSSLIGLGY description EUKARYOTIC_PORIN Eukaryotic mitochondrial porin signature. YqiDPdAcfsAKVNNssliGLgY source prosite : PS00558

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