eF-site ID 2rax-ABEFXY
PDB Code 2rax
Chain A, B, E, F, X, Y

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Title Crystal structure of Borealin (20-78) bound to Survivin (1-120)
Classification CELL CYCLE
Compound Baculoviral IAP repeat-containing protein 5
Source Homo sapiens (Human) (BOREA_HUMAN)
Sequence A:  TLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFI
HCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGC
AFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNN
B:  MKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEI
LRLPKALREMNWLDYFAL
E:  TLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFI
HCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGC
AFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNN
F:  MKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEI
LRLPKALREMNWLDYFAL
X:  TLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFI
HCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGC
AFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNN
Y:  MKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEI
LRLPKALREMNWLDYFAL
Description


Functional site
1) chain A
residue 57
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 341
source : AC1
2) chain A
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 341
source : AC1
3) chain A
residue 77
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 341
source : AC1
4) chain A
residue 84
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 341
source : AC1
5) chain E
residue 57
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 341
source : AC2
6) chain E
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 341
source : AC2
7) chain E
residue 77
type
sequence H
description BINDING SITE FOR RESIDUE ZN E 341
source : AC2
8) chain E
residue 84
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 341
source : AC2
9) chain X
residue 57
type
sequence C
description BINDING SITE FOR RESIDUE ZN X 341
source : AC3
10) chain X
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE ZN X 341
source : AC3
11) chain X
residue 77
type
sequence H
description BINDING SITE FOR RESIDUE ZN X 341
source : AC3
12) chain X
residue 84
type
sequence C
description BINDING SITE FOR RESIDUE ZN X 341
source : AC3
13) chain A
residue 20
type MOD_RES
sequence S
description Phosphoserine; by AURKC => ECO:0000269|PubMed:27332895
source Swiss-Prot : SWS_FT_FI2
14) chain E
residue 20
type MOD_RES
sequence S
description Phosphoserine; by AURKC => ECO:0000269|PubMed:27332895
source Swiss-Prot : SWS_FT_FI2
15) chain X
residue 20
type MOD_RES
sequence S
description Phosphoserine; by AURKC => ECO:0000269|PubMed:27332895
source Swiss-Prot : SWS_FT_FI2
16) chain A
residue 23
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20826784
source Swiss-Prot : SWS_FT_FI3
17) chain E
residue 115
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20826784
source Swiss-Prot : SWS_FT_FI3
18) chain X
residue 23
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20826784
source Swiss-Prot : SWS_FT_FI3
19) chain X
residue 90
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20826784
source Swiss-Prot : SWS_FT_FI3
20) chain X
residue 110
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20826784
source Swiss-Prot : SWS_FT_FI3
21) chain X
residue 112
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20826784
source Swiss-Prot : SWS_FT_FI3
22) chain X
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 E
residue 23
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20826784
source Swiss-Prot : SWS_FT_FI3
28) chain E
residue 90
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20826784
source Swiss-Prot : SWS_FT_FI3
29) chain E
residue 110
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20826784
source Swiss-Prot : SWS_FT_FI3
30) chain E
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 E
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 X
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
34) 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
35) chain E
residue 48
type MOD_RES
sequence T
description Phosphothreonine; by CK2; in vitro => ECO:0000269|PubMed:21252625
source Swiss-Prot : SWS_FT_FI5
36) chain X
residue 48
type MOD_RES
sequence T
description Phosphothreonine; by CK2; in vitro => ECO:0000269|PubMed:21252625
source Swiss-Prot : SWS_FT_FI5
37) chain A
residue 117
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:14610074
source Swiss-Prot : SWS_FT_FI6
38) chain E
residue 117
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:14610074
source Swiss-Prot : SWS_FT_FI6
39) chain X
residue 117
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:14610074
source Swiss-Prot : SWS_FT_FI6
40) chain A
residue 57
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
41) chain X
residue 60
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
42) chain X
residue 77
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
43) chain X
residue 84
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
44) chain A
residue 60
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
45) chain A
residue 77
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
46) chain A
residue 84
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
47) chain E
residue 57
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
48) chain E
residue 60
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
49) chain E
residue 77
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
50) chain E
residue 84
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1
51) chain X
residue 57
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:17956729, ECO:0007744|PDB:2QFA
source Swiss-Prot : SWS_FT_FI1

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