eF-site ID 5nvn-ABCD PDB Code 5nvn Chain A, B, C, D click to enlarge Title Crystal structure of the human 4EHP-4E-BP1 complex Classification TRANSLATION Compound Eukaryotic translation initiation factor 4E type 2 Source Homo sapiens (Human) (4EBP1_HUMAN) Sequence A:  GPHMLEAEHPLQYNYTFWYSRNIKQIGTFASVEQFWRFYS HMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRL RKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDI ISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTD SIKMP B:  TRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTS C:  GPHMLEAEHPLQYNYTFWYSRRNIKQIGTFASVEQFWRFY SHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIR LRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQED IISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHT DSIKMP D:  MTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTS Description Functional site 1) chain A residue 93 type sequence Q description binding site for residue FMT A 301 source : AC1 2) chain A residue 96 type sequence R description binding site for residue FMT A 301 source : AC1 3) chain B residue 72 type sequence P description binding site for residue FMT A 301 source : AC1 4) chain B residue 74 type sequence D description binding site for residue FMT A 301 source : AC1 5) chain C residue 198 type sequence D description binding site for residue FMT A 301 source : AC1 6) chain B residue 73 type sequence R description binding site for residue FMT C 301 source : AC2 7) chain C residue 199 type sequence T description binding site for residue FMT C 301 source : AC2 8) chain C residue 202 type sequence R description binding site for residue FMT C 301 source : AC2 9) chain B residue 73 type sequence R description binding site for residue FMT C 302 source : AC3 10) chain C residue 160 type sequence F description binding site for residue FMT C 302 source : AC3 11) chain C residue 161 type sequence M description binding site for residue FMT C 302 source : AC3 12) chain C residue 195 type sequence R description binding site for residue FMT C 302 source : AC3 13) chain C residue 199 type sequence T description binding site for residue FMT C 302 source : AC3 14) chain C residue 139 type sequence L description binding site for residue FMT C 303 source : AC4 15) chain C residue 140 type sequence R description binding site for residue FMT C 303 source : AC4 16) chain C residue 143 type sequence L description binding site for residue FMT C 303 source : AC4 17) chain C residue 177 type sequence E description binding site for residue FMT C 304 source : AC5 18) chain C residue 146 type sequence R description binding site for residue FMT C 305 source : AC6 19) chain C residue 150 type sequence N description binding site for residue FMT C 305 source : AC6 20) chain C residue 205 type sequence N description binding site for residue FMT C 305 source : AC6 21) chain D residue 56 type sequence R description binding site for residue FMT C 305 source : AC6 22) chain C residue 222 type sequence K description binding site for residue FMT C 306 source : AC7 23) chain A residue 112-135 type prosite sequence DFHLFKEGIKPMWEDDANKNGGKW description IF4E Eukaryotic initiation factor 4E signature. DFhlFKegIkPmWEDdanknGGKW source prosite : PS00813 24) chain B residue 50 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI1 25) chain D residue 50 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI1 26) chain C residue 222 type MOD_RES sequence K description Phosphothreonine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 54 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI2 28) chain D residue 54 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 174 type MOD_RES sequence R description Phosphotyrosine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI2 30) chain C residue 110 type MOD_RES sequence H description Phosphotyrosine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI2 31) chain C residue 124 type MOD_RES sequence W description Phosphotyrosine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI2 32) chain C residue 174 type MOD_RES sequence R description Phosphotyrosine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 65 type MOD_RES sequence S description Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR => ECO:0000269|PubMed:12588975, ECO:0000269|PubMed:12747827, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:25702871, ECO:0000269|PubMed:29750193, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 34) chain D residue 65 type MOD_RES sequence S description Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR => ECO:0000269|PubMed:12588975, ECO:0000269|PubMed:12747827, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:25702871, ECO:0000269|PubMed:29750193, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 35) chain B residue 70 type MOD_RES sequence T description Phosphothreonine; by MTOR => ECO:0000269|PubMed:12747827, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:25702871, ECO:0000269|PubMed:29750193, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI4 36) chain D residue 70 type MOD_RES sequence T description Phosphothreonine; by MTOR => ECO:0000269|PubMed:12747827, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:25702871, ECO:0000269|PubMed:29750193, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 77 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 38) chain D residue 77 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 39) chain C residue 222 type MOD_RES sequence K description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 40) chain B residue 83 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI6 41) chain D residue 83 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI6 42) chain B residue 57 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:22578813 source Swiss-Prot : SWS_FT_FI7 43) chain D residue 57 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:22578813 source Swiss-Prot : SWS_FT_FI7

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