eF-site ID 1q17-ABC
PDB Code 1q17
Chain A, B, C

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Title Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide
Classification HYDROLASE
Compound HST2 protein
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (HST2_YEAST)
Sequence A:  GMASMSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAGIS
TSCGIPDFRSPGTGLYHNLARLKLPYPEAVFDVDFFQSDP
LPFYTLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYTQN
IDTLERQAGVKDDLIIEAHGSFAHCHCIGCGKVYPPQVFK
SKLAEHPIKDFVKCDVCGELVKPAIVFFGEDLPDSFSETW
LNDSEWLREKIQPLVIVVGTSLAVYPFASLPEEIPRKVKR
VLCNLETVGDFKANKRPTDLIVHQYSDEFAEQLVEELGWQ
EDFEKILTAQ
B:  HHGMASMSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAG
ISTSCGIPDFRSPGTGLYHNLARLKLPYPEAVFDVDFFQS
DPLPFYTLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYT
QNIDTLERQAGVKDDLIIEAHGSFAHCHCIGCGKVYPPQV
FKSKLAEHPIKDFVKCDVCGELVKPAIVFFGEDLPDSFSE
TWLNDSEWLREKIPQQPLVIVVGTSLAVYPFASLPEEIPR
KVKRVLCNLETVGDFKANKRPTDLIVHQYSDEFAEQLVEE
LGWQEDFEKILTAQ
C:  HGMASMSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAGI
STSCGIPDFRSPGTGLYHNLARLKLPYPEAVFDVDFFQSD
PLPFYTLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYTQ
NIDTLERQAGVKDDLIIEAHGSFAHCHCIGCGKVYPPQVF
KSKLAEHPIKDFVKCDVCGELVKPAIVFFGEDLPDSFSET
WLNDSEWLREKIKHPQQPLVIVVGTSLAVYPFASLPEEIP
RKVKRVLCNLETVGDFKANKRPTDLIVHQYSDEFAEQLVE
ELGWQEDFEKILTAQ
Description


Functional site
1) chain A
residue 143
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 401
source : AC1
2) chain A
residue 146
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 401
source : AC1
3) chain A
residue 170
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 401
source : AC1
4) chain A
residue 173
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 401
source : AC1
5) chain B
residue 143
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 401
source : AC2
6) chain B
residue 146
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 401
source : AC2
7) chain B
residue 170
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 401
source : AC2
8) chain B
residue 173
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 401
source : AC2
9) chain C
residue 143
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 401
source : AC3
10) chain C
residue 146
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 401
source : AC3
11) chain C
residue 170
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 401
source : AC3
12) chain C
residue 173
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 401
source : AC3
13) chain C
residue 204
type
sequence R
description BINDING SITE FOR RESIDUE CL C 701
source : AC4
14) chain C
residue 240
type
sequence R
description BINDING SITE FOR RESIDUE CL C 701
source : AC4
15) chain B
residue 202
type
sequence W
description BINDING SITE FOR RESIDUE CL B 702
source : AC5
16) chain A
residue 204
type
sequence R
description BINDING SITE FOR RESIDUE CL A 703
source : AC6
17) chain A
residue 240
type
sequence R
description BINDING SITE FOR RESIDUE CL A 703
source : AC6
18) chain B
residue 204
type
sequence R
description BINDING SITE FOR RESIDUE CL B 704
source : AC7
19) chain B
residue 240
type
sequence R
description BINDING SITE FOR RESIDUE CL B 704
source : AC7
20) chain A
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
21) chain A
residue 33
type
sequence A
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
22) chain A
residue 34
type
sequence G
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
23) chain A
residue 37
type
sequence T
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
24) chain A
residue 43
type
sequence D
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
25) chain A
residue 44
type
sequence F
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
26) chain A
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
27) chain A
residue 52
type
sequence Y
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
28) chain A
residue 115
type
sequence Q
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
29) chain A
residue 135
type
sequence H
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
30) chain A
residue 223
type
sequence G
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
31) chain A
residue 224
type
sequence T
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
32) chain A
residue 225
type
sequence S
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
33) chain A
residue 228
type
sequence V
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
34) chain A
residue 248
type
sequence N
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
35) chain A
residue 249
type
sequence L
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
36) chain A
residue 250
type
sequence E
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
37) chain A
residue 268
type
sequence Q
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
38) chain A
residue 269
type
sequence Y
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
39) chain A
residue 270
type
sequence S
description BINDING SITE FOR RESIDUE APR A 1001
source : AC8
40) chain B
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
41) chain B
residue 33
type
sequence A
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
42) chain B
residue 34
type
sequence G
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
43) chain B
residue 37
type
sequence T
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
44) chain B
residue 43
type
sequence D
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
45) chain B
residue 44
type
sequence F
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
46) chain B
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
47) chain B
residue 52
type
sequence Y
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
48) chain B
residue 115
type
sequence Q
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
49) chain B
residue 135
type
sequence H
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
50) chain B
residue 223
type
sequence G
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
51) chain B
residue 224
type
sequence T
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
52) chain B
residue 225
type
sequence S
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
53) chain B
residue 228
type
sequence V
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
54) chain B
residue 248
type
sequence N
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
55) chain B
residue 249
type
sequence L
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
56) chain B
residue 268
type
sequence Q
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
57) chain B
residue 269
type
sequence Y
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
58) chain B
residue 270
type
sequence S
description BINDING SITE FOR RESIDUE APR B 1002
source : AC9
59) chain C
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
60) chain C
residue 33
type
sequence A
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
61) chain C
residue 34
type
sequence G
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
62) chain C
residue 37
type
sequence T
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
63) chain C
residue 43
type
sequence D
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
64) chain C
residue 44
type
sequence F
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
65) chain C
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
66) chain C
residue 52
type
sequence Y
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
67) chain C
residue 115
type
sequence Q
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
68) chain C
residue 135
type
sequence H
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
69) chain C
residue 223
type
sequence G
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
70) chain C
residue 224
type
sequence T
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
71) chain C
residue 225
type
sequence S
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
72) chain C
residue 228
type
sequence V
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
73) chain C
residue 248
type
sequence N
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
74) chain C
residue 249
type
sequence L
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
75) chain C
residue 268
type
sequence Q
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
76) chain C
residue 269
type
sequence Y
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
77) chain C
residue 270
type
sequence S
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
78) chain A
residue 42
type catalytic
sequence P
description 240
source MCSA : MCSA1
79) chain A
residue 43
type catalytic
sequence D
description 240
source MCSA : MCSA1
80) chain A
residue 44
type catalytic
sequence F
description 240
source MCSA : MCSA1
81) chain A
residue 45
type catalytic
sequence R
description 240
source MCSA : MCSA1
82) chain A
residue 116
type catalytic
sequence N
description 240
source MCSA : MCSA1
83) chain A
residue 118
type catalytic
sequence D
description 240
source MCSA : MCSA1
84) chain A
residue 135
type catalytic
sequence H
description 240
source MCSA : MCSA1
85) chain B
residue 42
type catalytic
sequence P
description 240
source MCSA : MCSA2
86) chain B
residue 43
type catalytic
sequence D
description 240
source MCSA : MCSA2
87) chain B
residue 44
type catalytic
sequence F
description 240
source MCSA : MCSA2
88) chain B
residue 45
type catalytic
sequence R
description 240
source MCSA : MCSA2
89) chain B
residue 116
type catalytic
sequence N
description 240
source MCSA : MCSA2
90) chain B
residue 118
type catalytic
sequence D
description 240
source MCSA : MCSA2
91) chain B
residue 135
type catalytic
sequence H
description 240
source MCSA : MCSA2
92) chain C
residue 42
type catalytic
sequence P
description 240
source MCSA : MCSA3
93) chain C
residue 43
type catalytic
sequence D
description 240
source MCSA : MCSA3
94) chain C
residue 44
type catalytic
sequence F
description 240
source MCSA : MCSA3
95) chain C
residue 45
type catalytic
sequence R
description 240
source MCSA : MCSA3
96) chain C
residue 116
type catalytic
sequence N
description 240
source MCSA : MCSA3
97) chain C
residue 118
type catalytic
sequence D
description 240
source MCSA : MCSA3
98) chain C
residue 135
type catalytic
sequence H
description 240
source MCSA : MCSA3
99) chain A
residue 143
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
100) chain C
residue 146
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
101) chain C
residue 170
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
102) chain C
residue 173
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
103) chain A
residue 146
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
104) chain A
residue 170
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
105) chain A
residue 173
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
106) chain B
residue 143
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
107) chain B
residue 146
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
108) chain B
residue 170
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
109) chain B
residue 173
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
110) chain C
residue 143
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592
source Swiss-Prot : SWS_FT_FI3
111) chain A
residue 135
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:20726530
source Swiss-Prot : SWS_FT_FI1
112) chain B
residue 135
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:20726530
source Swiss-Prot : SWS_FT_FI1
113) chain C
residue 135
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:20726530
source Swiss-Prot : SWS_FT_FI1
114) chain A
residue 32
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
115) chain B
residue 270
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
116) chain C
residue 32
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
117) chain C
residue 115
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
118) chain C
residue 223
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
119) chain C
residue 248
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
120) chain C
residue 270
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
121) chain A
residue 115
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
122) chain A
residue 223
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
123) chain A
residue 248
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
124) chain A
residue 270
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
125) chain B
residue 32
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
126) chain B
residue 115
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
127) chain B
residue 223
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
128) chain B
residue 248
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
129) chain A
residue 2
type MOD_RES
sequence S
description N-acetylserine => ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI4
130) chain B
residue 2
type MOD_RES
sequence S
description N-acetylserine => ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI4
131) chain C
residue 2
type MOD_RES
sequence S
description N-acetylserine => ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI4

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