eF-site ID 1jsa_8-A PDB Code 1jsa Model 8 Chain A click to enlarge Title MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES Classification CALCIUM BINDING Compound RECOVERIN Source null (RECO_BOVIN) Sequence A:  GNSKSGALSKEILEELQLNTKFTEEELSSWYQSFLKECPS GRITRQEFQTIYSKFFPEADPKAYAQHVFRSFDANSDGTL DFKEYVIALHMTSAGKTNQKLEWAFSLYDVDGNGTISKNE VLEIVTAIFKMISPEDTKHLPEDENTPEKRAEKIWGFFGK KDDDKLTEKEFIEGTLANKEILRLIQFE Description Functional site 1) chain A residue 73 type sequence D description BINDING SITE FOR RESIDUE CA A 500 source : AC1 2) chain A residue 75 type sequence N description BINDING SITE FOR RESIDUE CA A 500 source : AC1 3) chain A residue 77 type sequence D description BINDING SITE FOR RESIDUE CA A 500 source : AC1 4) chain A residue 79 type sequence T description BINDING SITE FOR RESIDUE CA A 500 source : AC1 5) chain A residue 84 type sequence E description BINDING SITE FOR RESIDUE CA A 500 source : AC1 6) chain A residue 109 type sequence D description BINDING SITE FOR RESIDUE CA A 501 source : AC2 7) chain A residue 111 type sequence D description BINDING SITE FOR RESIDUE CA A 501 source : AC2 8) chain A residue 113 type sequence N description BINDING SITE FOR RESIDUE CA A 501 source : AC2 9) chain A residue 115 type sequence T description BINDING SITE FOR RESIDUE CA A 501 source : AC2 10) chain A residue 120 type sequence E description BINDING SITE FOR RESIDUE CA A 501 source : AC2 11) chain A residue 1 type sequence G description BINDING SITE FOR RESIDUE MYR A 502 source : AC3 12) chain A residue 73-85 type prosite sequence DANSDGTLDFKEY description EF_HAND_1 EF-hand calcium-binding domain. DANSDGTLDfkEY source prosite : PS00018 13) chain A residue 109-121 type prosite sequence DVDGNGTISKNEV description EF_HAND_1 EF-hand calcium-binding domain. DANSDGTLDfkEY source prosite : PS00018 14) chain A residue 74 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0007744|PDB:4YI8 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 76 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0007744|PDB:4YI8 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 78 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0007744|PDB:4YI8 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 80 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0007744|PDB:4YI8 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 85 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0007744|PDB:4YI8 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 110 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:17015448, ECO:0000269|PubMed:17020884, ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:26584024, ECO:0000269|PubMed:7630423, ECO:0000269|PubMed:8242744, ECO:0007744|PDB:1OMR, ECO:0007744|PDB:1OMV, ECO:0007744|PDB:1REC, ECO:0007744|PDB:2HET, ECO:0007744|PDB:2I94, ECO:0007744|PDB:4M2O, ECO:0007744|PDB:4M2P, ECO:0007744|PDB:4M2Q, ECO:0007744|PDB:4MLW, ECO:0007744|PDB:4YI8, ECO:0007744|PDB:4YI9 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 112 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:17015448, ECO:0000269|PubMed:17020884, ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:26584024, ECO:0000269|PubMed:7630423, ECO:0000269|PubMed:8242744, ECO:0007744|PDB:1OMV, ECO:0007744|PDB:1REC, ECO:0007744|PDB:2HET, ECO:0007744|PDB:2I94, ECO:0007744|PDB:4M2O, ECO:0007744|PDB:4M2P, ECO:0007744|PDB:4M2Q, ECO:0007744|PDB:4MLW, ECO:0007744|PDB:4YI8, ECO:0007744|PDB:4YI9 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 114 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:17020884, ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:26584024, ECO:0000269|PubMed:7630423, ECO:0000269|PubMed:8242744, ECO:0007744|PDB:1OMR, ECO:0007744|PDB:1OMV, ECO:0007744|PDB:1REC, ECO:0007744|PDB:2I94, ECO:0007744|PDB:4M2O, ECO:0007744|PDB:4M2P, ECO:0007744|PDB:4M2Q, ECO:0007744|PDB:4MLW, ECO:0007744|PDB:4YI8, ECO:0007744|PDB:4YI9 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 116 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:17015448, ECO:0000269|PubMed:17020884, ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:26584024, ECO:0000269|PubMed:7630423, ECO:0000269|PubMed:8242744, ECO:0007744|PDB:1OMR, ECO:0007744|PDB:1OMV, ECO:0007744|PDB:1REC, ECO:0007744|PDB:2HET, ECO:0007744|PDB:2I94, ECO:0007744|PDB:4M2O, ECO:0007744|PDB:4M2P, ECO:0007744|PDB:4MLW, ECO:0007744|PDB:4YI8, ECO:0007744|PDB:4YI9 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 121 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:17015448, ECO:0000269|PubMed:17020884, ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:26584024, ECO:0000269|PubMed:7630423, ECO:0007744|PDB:1OMR, ECO:0007744|PDB:1OMV, ECO:0007744|PDB:2HET, ECO:0007744|PDB:2I94, ECO:0007744|PDB:4M2O, ECO:0007744|PDB:4M2P, ECO:0007744|PDB:4M2Q, ECO:0007744|PDB:4MLW, ECO:0007744|PDB:4YI8 source Swiss-Prot : SWS_FT_FI6 24) chain A residue 39 type MOD_RES sequence P description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:25772009 source Swiss-Prot : SWS_FT_FI8 25) chain A residue 2 type LIPID sequence N description N-myristoyl glycine => ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:1386601, ECO:0000269|PubMed:7630423 source Swiss-Prot : SWS_FT_FI9

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