eF-site ID 4aq3-ABCDEF PDB Code 4aq3 Chain A, B, C, D, E, F click to enlarge Title HUMAN BCL-2 WITH PHENYLACYLSULFONAMIDE INHIBITOR Classification APOPTOSIS Compound APOPTOSIS REGULATOR BCL-2, BCL-2-LIKE PROTEIN 1 Source Homo sapiens (Human) (BCLX_HUMAN) Sequence A:  YDNREIVMKYIHYKLSQRGYEWDVVHLALRQAGDDFSRRY RGDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIV AFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTW IQDNGGWDAFVELYG B:  YDNREIVMKYIHYKLSQRGYEWDVVHLALRQAGDDFSRRY RGDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIV AFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTW IQDNGGWDAFVELYG C:  YDNREIVMKYIHYKLSQRGYEWDVVHLALRQAGDDFSRRY RGDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIV AFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTW IQDNGGWDAFVELYG D:  YDNREIVMKYIHYKLSQRGYEWDSEVVHLALRQAGDDFSR RYRGDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGR IVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLH TWIQDNGGWDAFVELYG E:  DNREIVMKYIHYKLSQRGYEWDAVVHLALRQAGDDFSRRY RGDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIV AFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTW IQDNGGWDAFVELYG F:  YDNREIVMKYIHYKLSQRGYEWDAEVVHLALRQAGDDFSR RYRGDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGR IVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLH TWIQDNGGWDAFVELYG Description Functional site 1) chain A residue 67 type sequence Y description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 2) chain A residue 70 type sequence D description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 3) chain A residue 74 type sequence M description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 4) chain A residue 95 type sequence E description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 5) chain A residue 96 type sequence L description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 6) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 7) chain E residue 58 type sequence Q description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 8) chain E residue 160 type sequence L description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 9) chain E residue 161 type sequence Y description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 10) chain E residue 162 type sequence G description BINDING SITE FOR RESIDUE 398 A 1163 source : AC1 11) chain B residue 63 type sequence F description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 12) chain B residue 67 type sequence Y description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 13) chain B residue 70 type sequence D description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 14) chain B residue 71 type sequence F description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 15) chain B residue 74 type sequence M description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 16) chain B residue 92 type sequence V description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 17) chain B residue 95 type sequence E description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 18) chain B residue 104 type sequence G description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 19) chain B residue 108 type sequence A description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 20) chain B residue 112 type sequence F description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 21) chain B residue 161 type sequence Y description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 22) chain D residue 58 type sequence Q description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 23) chain D residue 161 type sequence Y description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 24) chain D residue 162 type sequence G description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 25) chain E residue 82 type sequence P description BINDING SITE FOR RESIDUE 398 B 1163 source : AC2 26) chain C residue 63 type sequence F description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 27) chain C residue 67 type sequence Y description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 28) chain C residue 70 type sequence D description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 29) chain C residue 74 type sequence M description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 30) chain C residue 95 type sequence E description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 31) chain C residue 96 type sequence L description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 32) chain C residue 161 type sequence Y description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 33) chain D residue 82 type sequence P description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 34) chain F residue 58 type sequence Q description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 35) chain F residue 161 type sequence Y description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 36) chain F residue 162 type sequence G description BINDING SITE FOR RESIDUE 398 C 1163 source : AC3 37) chain A residue 82 type sequence P description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 38) chain B residue 58 type sequence Q description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 39) chain B residue 160 type sequence L description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 40) chain B residue 161 type sequence Y description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 41) chain B residue 162 type sequence G description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 42) chain D residue 63 type sequence F description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 43) chain D residue 67 type sequence Y description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 44) chain D residue 70 type sequence D description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 45) chain D residue 74 type sequence M description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 46) chain D residue 95 type sequence E description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 47) chain D residue 108 type sequence A description BINDING SITE FOR RESIDUE 398 D 1163 source : AC4 48) chain A residue 58 type sequence Q description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 49) chain A residue 160 type sequence L description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 50) chain A residue 161 type sequence Y description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 51) chain A residue 162 type sequence G description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 52) chain E residue 63 type sequence F description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 53) chain E residue 67 type sequence Y description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 54) chain E residue 70 type sequence D description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 55) chain E residue 74 type sequence M description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 56) chain E residue 92 type sequence V description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 57) chain E residue 95 type sequence E description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 58) chain E residue 108 type sequence A description BINDING SITE FOR RESIDUE 398 E 1163 source : AC5 59) chain B residue 83 type sequence F description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 60) chain C residue 58 type sequence Q description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 61) chain C residue 160 type sequence L description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 62) chain C residue 161 type sequence Y description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 63) chain C residue 162 type sequence G description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 64) chain F residue 63 type sequence F description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 65) chain F residue 67 type sequence Y description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 66) chain F residue 70 type sequence D description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 67) chain F residue 92 type sequence V description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 68) chain F residue 95 type sequence E description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 69) chain F residue 108 type sequence A description BINDING SITE FOR RESIDUE 398 F 1163 source : AC6 70) chain A residue 96-114 type prosite sequence LFRDGVNWGRIVAFFEFGG description BH1 Apoptosis regulator, Bcl-2 family BH1 motif signature. LFrDGv.NWGRIVAFFeFGG source prosite : PS01080 71) chain A residue 147-158 type prosite sequence WIQDNGGWDAFV description BH2 Apoptosis regulator, Bcl-2 family BH2 motif signature. WIqdnGGWDaFV source prosite : PS01258 72) chain A residue 52-66 type prosite sequence VHLALRQAGDDFSRR description BH3 Apoptosis regulator, Bcl-2 family BH3 motif signature. VhlaLRqAGDDFSRR source prosite : PS01259 73) chain A residue 10-30 type prosite sequence DNREIVMKYIHYKLSQRGYEW description BH4_1 Apoptosis regulator, Bcl-2 family BH4 motif signature. DNREIVmKYIHYKLSQRGYeW source prosite : PS01260 74) chain A residue 54 type MOD_RES sequence L description Phosphothreonine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI1 75) chain B residue 54 type MOD_RES sequence L description Phosphothreonine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI1 76) chain C residue 54 type MOD_RES sequence L description Phosphothreonine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI1 77) chain D residue 54 type MOD_RES sequence L description Phosphothreonine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI1 78) chain E residue 54 type MOD_RES sequence L description Phosphothreonine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI1 79) chain F residue 54 type MOD_RES sequence L description Phosphothreonine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI1 80) chain A residue 55 type MOD_RES sequence A description Phosphoserine; by MAPK8 and PKC => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI2 81) chain B residue 55 type MOD_RES sequence A description Phosphoserine; by MAPK8 and PKC => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI2 82) chain C residue 55 type MOD_RES sequence A description Phosphoserine; by MAPK8 and PKC => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI2 83) chain D residue 55 type MOD_RES sequence A description Phosphoserine; by MAPK8 and PKC => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI2 84) chain E residue 55 type MOD_RES sequence A description Phosphoserine; by MAPK8 and PKC => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI2 85) chain F residue 55 type MOD_RES sequence A description Phosphoserine; by MAPK8 and PKC => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI2 86) chain A residue 72 type MOD_RES sequence A description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI3 87) chain B residue 72 type MOD_RES sequence A description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI3 88) chain C residue 72 type MOD_RES sequence A description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI3 89) chain D residue 72 type MOD_RES sequence A description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI3 90) chain E residue 72 type MOD_RES sequence A description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI3 91) chain F residue 72 type MOD_RES sequence A description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:18570871 source Swiss-Prot : SWS_FT_FI3

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