eF-site ID 1q17-C
PDB Code 1q17
Chain 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 C:  HGMASMSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAGI
STSCGIPDFRSPGTGLYHNLARLKLPYPEAVFDVDFFQSD
PLPFYTLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYTQ
NIDTLERQAGVKDDLIIEAHGSFAHCHCIGCGKVYPPQVF
KSKLAEHPIKDFVKCDVCGELVKPAIVFFGEDLPDSFSET
WLNDSEWLREKIKHPQQPLVIVVGTSLAVYPFASLPEEIP
RKVKRVLCNLETVGDFKANKRPTDLIVHQYSDEFAEQLVE
ELGWQEDFEKILTAQ
Description


Functional site
1) chain C
residue 143
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 401
source : AC3
2) chain C
residue 146
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 401
source : AC3
3) chain C
residue 170
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 401
source : AC3
4) chain C
residue 173
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 401
source : AC3
5) chain C
residue 204
type
sequence R
description BINDING SITE FOR RESIDUE CL C 701
source : AC4
6) chain C
residue 240
type
sequence R
description BINDING SITE FOR RESIDUE CL C 701
source : AC4
7) chain C
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
8) chain C
residue 33
type
sequence A
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
9) chain C
residue 34
type
sequence G
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
10) chain C
residue 37
type
sequence T
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
11) chain C
residue 43
type
sequence D
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
12) chain C
residue 44
type
sequence F
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
13) chain C
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
14) chain C
residue 52
type
sequence Y
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
15) chain C
residue 115
type
sequence Q
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
16) chain C
residue 135
type
sequence H
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
17) chain C
residue 223
type
sequence G
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
18) chain C
residue 224
type
sequence T
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
19) chain C
residue 225
type
sequence S
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
20) chain C
residue 228
type
sequence V
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
21) chain C
residue 248
type
sequence N
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
22) chain C
residue 249
type
sequence L
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
23) chain C
residue 268
type
sequence Q
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
24) chain C
residue 269
type
sequence Y
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
25) chain C
residue 270
type
sequence S
description BINDING SITE FOR RESIDUE APR C 1003
source : BC1
26) chain C
residue 42
type catalytic
sequence P
description 240
source MCSA : MCSA3
27) chain C
residue 43
type catalytic
sequence D
description 240
source MCSA : MCSA3
28) chain C
residue 44
type catalytic
sequence F
description 240
source MCSA : MCSA3
29) chain C
residue 45
type catalytic
sequence R
description 240
source MCSA : MCSA3
30) chain C
residue 116
type catalytic
sequence N
description 240
source MCSA : MCSA3
31) chain C
residue 118
type catalytic
sequence D
description 240
source MCSA : MCSA3
32) chain C
residue 135
type catalytic
sequence H
description 240
source MCSA : MCSA3
33) 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
34) 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
35) 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
36) 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
37) 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
38) chain C
residue 32
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
39) chain C
residue 115
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
40) chain C
residue 223
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
41) chain C
residue 248
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
42) chain C
residue 270
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415
source Swiss-Prot : SWS_FT_FI2
43) 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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