eF-site ID 3rdh-ABCD
PDB Code 3rdh
Chain A, B, C, D

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Title X-ray induced covalent inhibition of 14-3-3
Classification SIGNALING PROTEIN/INHIBITOR
Compound 14-3-3 protein zeta/delta
Source Homo sapiens (Human) (1433Z_HUMAN)
Sequence A:  GSHMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELS
NEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQ
MAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVF
YLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISK
KEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFD
EAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS
B:  GSHMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELS
NEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQ
MAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVF
YLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISK
KEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFD
EAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS
C:  GSHMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELS
NEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQ
MAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVF
YLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISK
KEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFD
EAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS
D:  GSHMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELS
NEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQ
MAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVF
YLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISK
KEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFD
EAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS
Description


Functional site
1) chain A
residue 120
type
sequence K
description BINDING SITE FOR RESIDUE 3RD A 246
source : AC1
2) chain A
residue 172
type
sequence L
description BINDING SITE FOR RESIDUE 3RD A 246
source : AC1
3) chain A
residue 173
type
sequence N
description BINDING SITE FOR RESIDUE 3RD A 246
source : AC1
4) chain A
residue 217
type
sequence I
description BINDING SITE FOR RESIDUE 3RD A 246
source : AC1
5) chain A
residue 220
type
sequence L
description BINDING SITE FOR RESIDUE 3RD A 246
source : AC1
6) chain A
residue -2
type
sequence G
description BINDING SITE FOR RESIDUE NI A 247
source : AC2
7) chain A
residue -1
type
sequence S
description BINDING SITE FOR RESIDUE NI A 247
source : AC2
8) chain A
residue 0
type
sequence H
description BINDING SITE FOR RESIDUE NI A 247
source : AC2
9) chain A
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE NI A 247
source : AC2
10) chain B
residue 49
type
sequence K
description BINDING SITE FOR RESIDUE 3RD B 246
source : AC3
11) chain B
residue 120
type
sequence K
description BINDING SITE FOR RESIDUE 3RD B 246
source : AC3
12) chain B
residue 169
type
sequence G
description BINDING SITE FOR RESIDUE 3RD B 246
source : AC3
13) chain B
residue 173
type
sequence N
description BINDING SITE FOR RESIDUE 3RD B 246
source : AC3
14) chain B
residue 217
type
sequence I
description BINDING SITE FOR RESIDUE 3RD B 246
source : AC3
15) chain B
residue -1
type
sequence S
description BINDING SITE FOR RESIDUE NI B 247
source : AC4
16) chain B
residue -2
type
sequence G
description BINDING SITE FOR RESIDUE NI B 247
source : AC4
17) chain B
residue 0
type
sequence H
description BINDING SITE FOR RESIDUE NI B 247
source : AC4
18) chain B
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE NI B 247
source : AC4
19) chain C
residue 49
type
sequence K
description BINDING SITE FOR RESIDUE 3RD C 246
source : AC5
20) chain C
residue 120
type
sequence K
description BINDING SITE FOR RESIDUE 3RD C 246
source : AC5
21) chain C
residue 169
type
sequence G
description BINDING SITE FOR RESIDUE 3RD C 246
source : AC5
22) chain C
residue 173
type
sequence N
description BINDING SITE FOR RESIDUE 3RD C 246
source : AC5
23) chain C
residue -2
type
sequence G
description BINDING SITE FOR RESIDUE NI C 247
source : AC6
24) chain C
residue -1
type
sequence S
description BINDING SITE FOR RESIDUE NI C 247
source : AC6
25) chain C
residue 0
type
sequence H
description BINDING SITE FOR RESIDUE NI C 247
source : AC6
26) chain C
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE NI C 247
source : AC6
27) chain D
residue 49
type
sequence K
description BINDING SITE FOR RESIDUE 3RD D 246
source : AC7
28) chain D
residue 120
type
sequence K
description BINDING SITE FOR RESIDUE 3RD D 246
source : AC7
29) chain D
residue 169
type
sequence G
description BINDING SITE FOR RESIDUE 3RD D 246
source : AC7
30) chain D
residue 173
type
sequence N
description BINDING SITE FOR RESIDUE 3RD D 246
source : AC7
31) chain D
residue -1
type
sequence S
description BINDING SITE FOR RESIDUE NI D 247
source : AC8
32) chain D
residue -2
type
sequence G
description BINDING SITE FOR RESIDUE NI D 247
source : AC8
33) chain D
residue 0
type
sequence H
description BINDING SITE FOR RESIDUE NI D 247
source : AC8
34) chain D
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE NI D 247
source : AC8
35) chain A
residue 41-51
type prosite
sequence RNLLSVAYKNV
description 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
source prosite : PS00796
36) chain A
residue 211-230
type prosite
sequence YKDSTLIMQLLRDNLTLWTS
description 1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
source prosite : PS00797
37) chain A
residue 56
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103
source Swiss-Prot : SWS_FT_FI1
38) chain A
residue 127
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103
source Swiss-Prot : SWS_FT_FI1
39) chain B
residue 56
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103
source Swiss-Prot : SWS_FT_FI1
40) chain B
residue 127
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103
source Swiss-Prot : SWS_FT_FI1
41) chain C
residue 56
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103
source Swiss-Prot : SWS_FT_FI1
42) chain C
residue 127
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103
source Swiss-Prot : SWS_FT_FI1
43) chain D
residue 56
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103
source Swiss-Prot : SWS_FT_FI1
44) chain D
residue 127
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103
source Swiss-Prot : SWS_FT_FI1
45) chain A
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
46) chain B
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
47) chain C
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
48) chain D
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
49) chain A
residue 3
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3
50) chain A
residue 68
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3
51) chain B
residue 3
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3
52) chain B
residue 68
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3
53) chain C
residue 3
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3
54) chain C
residue 68
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3
55) chain D
residue 3
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3
56) chain D
residue 68
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3
57) chain A
residue 58
type MOD_RES
sequence S
description Phosphoserine; by PKA and PKB/AKT1 => ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338
source Swiss-Prot : SWS_FT_FI4
58) chain B
residue 58
type MOD_RES
sequence S
description Phosphoserine; by PKA and PKB/AKT1 => ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338
source Swiss-Prot : SWS_FT_FI4
59) chain C
residue 58
type MOD_RES
sequence S
description Phosphoserine; by PKA and PKB/AKT1 => ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338
source Swiss-Prot : SWS_FT_FI4
60) chain D
residue 58
type MOD_RES
sequence S
description Phosphoserine; by PKA and PKB/AKT1 => ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338
source Swiss-Prot : SWS_FT_FI4
61) chain A
residue 184
type MOD_RES
sequence S
description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159
source Swiss-Prot : SWS_FT_FI5
62) chain B
residue 184
type MOD_RES
sequence S
description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159
source Swiss-Prot : SWS_FT_FI5
63) chain C
residue 184
type MOD_RES
sequence S
description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159
source Swiss-Prot : SWS_FT_FI5
64) chain D
residue 184
type MOD_RES
sequence S
description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159
source Swiss-Prot : SWS_FT_FI5
65) chain A
residue 207
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI6
66) chain B
residue 207
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI6
67) chain C
residue 207
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI6
68) chain D
residue 207
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI6
69) chain A
residue 210
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P63102
source Swiss-Prot : SWS_FT_FI7
70) chain B
residue 210
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P63102
source Swiss-Prot : SWS_FT_FI7
71) chain C
residue 210
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P63102
source Swiss-Prot : SWS_FT_FI7
72) chain D
residue 210
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P63102
source Swiss-Prot : SWS_FT_FI7

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