eF-site ID 1m2n-AB
PDB Code 1m2n
Chain A, B

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Title Sir2 homologues (D102G/F159A/R170A) mutant-2'-O-acetyl ADP ribose complex
Classification GENE REGULATION
Compound Silent Information Regulator 2
Source null (NPD1_ARCFU)
Sequence A:  MDEKLLKTIAESKYLVALTGAGVSAESGIPTFRGKDGLWN
RYRPEELANPQAFAKDPEKVWKWYAWRMEKVFNAQPNKAH
QAFAELERLGVLKCLITQNVDGLHERAGSRNVIHLHGSLR
VVRCTSCNNSFEVESAPKIPPLPKCDKCGSLLRPGVVWAG
EMLPPDVLDAAMREVERADVIIVAGTSAVVQPAASLPLIV
KQRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHV
RKALSLKLN
B:  MDEKLLKTIAESKYLVALTGAGVSAESGIPTFRGKDGLWN
RYRPEELANPQAFAKDPEKVWKWYAWRMEKVFNAQPNKAH
QAFAELERLGVLKCLITQNVDGLHERAGSRNVIHLHGSLR
VVRCTSCNNSFEVESAPKIPPLPKCDKCGSLLRPGVVWAG
EMLPPDVLDAAMREVERADVIIVAGTSAVVQPAASLPLIV
KQRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHV
RKALSLKLN
Description


Functional site
1) chain A
residue 124
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 999
source : AC1
2) chain A
residue 127
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 999
source : AC1
3) chain A
residue 145
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 999
source : AC1
4) chain A
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 999
source : AC1
5) chain B
residue 124
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 999
source : AC2
6) chain B
residue 127
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 999
source : AC2
7) chain B
residue 145
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 999
source : AC2
8) chain B
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 999
source : AC2
9) chain B
residue 150
type
sequence S
description BINDING SITE FOR RESIDUE ZN B 999
source : AC2
10) chain A
residue 20
type
sequence G
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
11) chain A
residue 21
type
sequence A
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
12) chain A
residue 22
type
sequence G
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
13) chain A
residue 26
type
sequence E
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
14) chain A
residue 31
type
sequence T
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
15) chain A
residue 32
type
sequence F
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
16) chain A
residue 33
type
sequence R
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
17) chain A
residue 98
type
sequence Q
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
18) chain A
residue 116
type
sequence H
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
19) chain A
residue 157
type
sequence V
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
20) chain A
residue 185
type
sequence G
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
21) chain A
residue 186
type
sequence T
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
22) chain A
residue 187
type
sequence S
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
23) chain A
residue 190
type
sequence V
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
24) chain A
residue 211
type
sequence N
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
25) chain A
residue 212
type
sequence P
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
26) chain A
residue 228
type
sequence K
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
27) chain A
residue 229
type
sequence A
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
28) chain A
residue 247
type
sequence K
description BINDING SITE FOR RESIDUE OAD B 1001
source : AC3
29) chain B
residue 20
type
sequence G
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
30) chain B
residue 21
type
sequence A
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
31) chain B
residue 22
type
sequence G
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
32) chain B
residue 26
type
sequence E
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
33) chain B
residue 31
type
sequence T
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
34) chain B
residue 32
type
sequence F
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
35) chain B
residue 33
type
sequence R
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
36) chain B
residue 98
type
sequence Q
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
37) chain B
residue 116
type
sequence H
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
38) chain B
residue 157
type
sequence V
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
39) chain B
residue 185
type
sequence G
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
40) chain B
residue 186
type
sequence T
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
41) chain B
residue 187
type
sequence S
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
42) chain B
residue 190
type
sequence V
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
43) chain B
residue 211
type
sequence N
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
44) chain B
residue 212
type
sequence P
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
45) chain B
residue 213
type
sequence D
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
46) chain B
residue 228
type
sequence K
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
47) chain B
residue 229
type
sequence A
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
48) chain B
residue 247
type
sequence K
description BINDING SITE FOR RESIDUE OAD B 2001
source : AC4
49) chain A
residue 116
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236
source Swiss-Prot : SWS_FT_FI1
50) chain B
residue 116
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236
source Swiss-Prot : SWS_FT_FI1
51) chain A
residue 64
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121
source Swiss-Prot : SWS_FT_FI3
52) chain A
residue 67
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121
source Swiss-Prot : SWS_FT_FI3
53) chain B
residue 64
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121
source Swiss-Prot : SWS_FT_FI3
54) chain B
residue 67
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121
source Swiss-Prot : SWS_FT_FI3
55) chain A
residue 124
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
source Swiss-Prot : SWS_FT_FI4
56) chain A
residue 127
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
source Swiss-Prot : SWS_FT_FI4
57) chain A
residue 145
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
source Swiss-Prot : SWS_FT_FI4
58) chain A
residue 148
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
source Swiss-Prot : SWS_FT_FI4
59) chain B
residue 124
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
source Swiss-Prot : SWS_FT_FI4
60) chain B
residue 127
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
source Swiss-Prot : SWS_FT_FI4
61) chain B
residue 145
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
source Swiss-Prot : SWS_FT_FI4
62) chain B
residue 148
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
source Swiss-Prot : SWS_FT_FI4
63) chain A
residue 98
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2
64) chain B
residue 229
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2
65) chain A
residue 185
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2
66) chain A
residue 211
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2
67) chain A
residue 229
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2
68) chain B
residue 20
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2
69) chain B
residue 98
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2
70) chain B
residue 185
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2
71) chain B
residue 211
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2
72) chain A
residue 20
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
source Swiss-Prot : SWS_FT_FI2

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