eF-site ID 3ten-ABCDEFGH
PDB Code 3ten
Chain A, B, C, D, E, F, G, H

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Title Holo form of carbon disulfide hydrolase
Classification HYDROLASE
Compound CS2 hydrolase
Source ORGANISM_SCIENTIFIC: Acidianus sp. A1-3;
Sequence A:  SEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHI
EQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKE
IIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLP
AFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHP
LIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIV
K
B:  SEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHI
EQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKE
IIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLP
AFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHP
LIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIV
K
C:  SEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHI
EQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKE
IIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLP
AFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHP
LIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIV
K
D:  SEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHI
EQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKE
IIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLP
AFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHP
LIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIV
K
E:  SEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHI
EQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKE
IIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLP
AFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHP
LIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIV
K
F:  SEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHI
EQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKE
IIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLP
AFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHP
LIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIV
K
G:  SEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHI
EQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKE
IIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLP
AFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHP
LIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIV
K
H:  SEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHI
EQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKE
IIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLP
AFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHP
LIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIV
K
Description


Functional site
1) chain A
residue 35
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 205
source : AC1
2) chain A
residue 88
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 205
source : AC1
3) chain A
residue 91
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 205
source : AC1
4) chain B
residue 35
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 205
source : AC2
5) chain B
residue 88
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 205
source : AC2
6) chain B
residue 91
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 205
source : AC2
7) chain C
residue 35
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 205
source : AC3
8) chain C
residue 88
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 205
source : AC3
9) chain C
residue 91
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 205
source : AC3
10) chain D
residue 35
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 205
source : AC4
11) chain D
residue 88
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 205
source : AC4
12) chain D
residue 91
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 205
source : AC4
13) chain E
residue 35
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 205
source : AC5
14) chain E
residue 88
type
sequence H
description BINDING SITE FOR RESIDUE ZN E 205
source : AC5
15) chain E
residue 91
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 205
source : AC5
16) chain F
residue 35
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 205
source : AC6
17) chain F
residue 88
type
sequence H
description BINDING SITE FOR RESIDUE ZN F 205
source : AC6
18) chain F
residue 91
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 205
source : AC6
19) chain G
residue 35
type
sequence C
description BINDING SITE FOR RESIDUE ZN G 205
source : AC7
20) chain G
residue 88
type
sequence H
description BINDING SITE FOR RESIDUE ZN G 205
source : AC7
21) chain G
residue 91
type
sequence C
description BINDING SITE FOR RESIDUE ZN G 205
source : AC7
22) chain H
residue 35
type
sequence C
description BINDING SITE FOR RESIDUE ZN H 205
source : AC8
23) chain H
residue 88
type
sequence H
description BINDING SITE FOR RESIDUE ZN H 205
source : AC8
24) chain H
residue 91
type
sequence C
description BINDING SITE FOR RESIDUE ZN H 205
source : AC8
25) chain A
residue 35
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
26) chain D
residue 35
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
27) chain D
residue 88
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
28) chain D
residue 91
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
29) chain E
residue 35
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
30) chain E
residue 88
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
31) chain E
residue 91
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
32) chain F
residue 35
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
33) chain F
residue 88
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
34) chain F
residue 91
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
35) chain G
residue 35
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
36) chain A
residue 88
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
37) chain G
residue 88
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
38) chain G
residue 91
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
39) chain H
residue 35
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
40) chain H
residue 88
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
41) chain H
residue 91
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
42) chain A
residue 91
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
43) chain B
residue 35
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
44) chain B
residue 88
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
45) chain B
residue 91
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
46) chain C
residue 35
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
47) chain C
residue 88
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1
48) chain C
residue 91
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:22012399, ECO:0000312|PDB:3TEN
source Swiss-Prot : SWS_FT_FI1

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