eF-site ID 1xox-AB PDB Code 1xox Chain A, B click to enlarge Title SOLUTION STRUCTURE OF HUMAN SURVIVIN Classification APOPTOSIS Compound Apoptosis inhibitor survivin Source Homo sapiens (Human) (BIRC5_HUMAN) Sequence A:  MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAE AGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKH SSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKET B:  MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAE AGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKH SSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKET Description Functional site 1) chain B residue 57 type sequence C description BINDING SITE FOR RESIDUE ZN B 998 source : AC1 2) chain B residue 58 type sequence F description BINDING SITE FOR RESIDUE ZN B 998 source : AC1 3) chain B residue 60 type sequence C description BINDING SITE FOR RESIDUE ZN B 998 source : AC1 4) chain B residue 77 type sequence H description BINDING SITE FOR RESIDUE ZN B 998 source : AC1 5) chain B residue 84 type sequence C description BINDING SITE FOR RESIDUE ZN B 998 source : AC1 6) chain A residue 57 type sequence C description BINDING SITE FOR RESIDUE ZN A 999 source : AC2 7) chain A residue 58 type sequence F description BINDING SITE FOR RESIDUE ZN A 999 source : AC2 8) chain A residue 60 type sequence C description BINDING SITE FOR RESIDUE ZN A 999 source : AC2 9) chain A residue 77 type sequence H description BINDING SITE FOR RESIDUE ZN A 999 source : AC2 10) chain A residue 84 type sequence C description BINDING SITE FOR RESIDUE ZN A 999 source : AC2 11) chain A residue 20 type MOD_RES sequence S description Phosphoserine; by AURKC => ECO:0000269|PubMed:27332895 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 20 type MOD_RES sequence S description Phosphoserine; by AURKC => ECO:0000269|PubMed:27332895 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 57 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA source Swiss-Prot : SWS_FT_FI1 14) chain A residue 60 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA source Swiss-Prot : SWS_FT_FI1 15) chain A residue 77 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA source Swiss-Prot : SWS_FT_FI1 16) chain A residue 84 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA source Swiss-Prot : SWS_FT_FI1 17) chain B residue 57 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA source Swiss-Prot : SWS_FT_FI1 18) chain B residue 60 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA source Swiss-Prot : SWS_FT_FI1 19) chain B residue 77 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA source Swiss-Prot : SWS_FT_FI1 20) chain B residue 84 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA source Swiss-Prot : SWS_FT_FI1 21) chain A residue 23 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 115 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 90 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 110 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 112 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 115 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 23 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 90 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 110 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 112 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20826784 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 34 type MOD_RES sequence T description Phosphothreonine; by CDK1 and CDK15 => ECO:0000269|PubMed:11069302, ECO:0000269|PubMed:24866247, ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI4 32) chain B residue 34 type MOD_RES sequence T description Phosphothreonine; by CDK1 and CDK15 => ECO:0000269|PubMed:11069302, ECO:0000269|PubMed:24866247, ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 48 type MOD_RES sequence T description Phosphothreonine; by CK2; in vitro => ECO:0000269|PubMed:21252625 source Swiss-Prot : SWS_FT_FI5 34) chain B residue 48 type MOD_RES sequence T description Phosphothreonine; by CK2; in vitro => ECO:0000269|PubMed:21252625 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 117 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:14610074 source Swiss-Prot : SWS_FT_FI6 36) chain B residue 117 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:14610074 source Swiss-Prot : SWS_FT_FI6

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