eF-site ID 1rk4-AB PDB Code 1rk4 Chain A, B click to enlarge Title Crystal Structure of a Soluble Dimeric Form of Oxidised CLIC1 Classification ION TRANSPORT/MEMBRANE PROTEIN Compound CHLORIDE INTRACELLULAR CHANNEL PROTEIN 1 Source Homo sapiens (Human) (CLIC1_HUMAN) Sequence A:  GNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPG GQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNP ESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLD NYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLL PKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFAS TCPDDEEIELAYE B:  GNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPG GQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNP ESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLD NYLTSPLPEEVDGVSQRKFLDGNELTLADCNLLPKLHIVQ VVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEE IELAYE Description Functional site 1) chain A residue 24 type MOD_RES sequence C description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:14613939 source Swiss-Prot : SWS_FT_FI5 2) chain B residue 24 type MOD_RES sequence C description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:14613939 source Swiss-Prot : SWS_FT_FI5 3) chain A residue 121 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 4) chain A residue 156 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 5) chain A residue 211 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 6) chain B residue 121 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 7) chain B residue 211 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 8) chain A residue 26-46 type TRANSMEM sequence FSQRLFMVLWLKGVTFNVTTV description Helical; Note=After insertion into the membrane => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 9) chain B residue 26-46 type TRANSMEM sequence FSQRLFMVLWLKGVTFNVTTV description Helical; Note=After insertion into the membrane => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 64 type BINDING sequence L description BINDING => ECO:0000269|PubMed:11551966 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 77 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11551966 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 64 type BINDING sequence L description BINDING => ECO:0000269|PubMed:11551966 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 77 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11551966 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 233 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1Q5 source Swiss-Prot : SWS_FT_FI7 15) chain B residue 233 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1Q5 source Swiss-Prot : SWS_FT_FI7 16) chain A residue 119 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 18) chain B residue 119 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 19) chain B residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4

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