|
eF-site ID
|
1dzu-P |
PDB Code
|
1dzu |
Chain
|
P |
|
click to enlarge
|
|
Title
|
L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant T26A |
Classification
|
LYASE (ALDEHYDE) |
Compound
|
L-fuculose phosphate aldolase |
Source
|
(A0A037YR34_ECOLX) |
|
Sequence
|
P: |
MERNKLARQIIDTCLEMTRLGLNQGAAGNVSVRYQDGMLI
TPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSEWRFHMAA
YQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGG
NSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIAC
EVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIA
VVLEKFKTY
|
|
Description
|
(1) |
L-FUCULOSE-1-PHOSPHATE ALDOLASE (E.C.4.1.2.17)
|
|
Functional site
|
|
1)
|
chain |
P |
residue |
73 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN P 999
|
source |
: AC1
|
|
2)
|
chain |
P |
residue |
92 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN P 999
|
source |
: AC1
|
|
3)
|
chain |
P |
residue |
94 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN P 999
|
source |
: AC1
|
|
4)
|
chain |
P |
residue |
113 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE ZN P 999
|
source |
: AC1
|
|
5)
|
chain |
P |
residue |
155 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN P 999
|
source |
: AC1
|
|
6)
|
chain |
P |
residue |
29 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE SO4 P 300
|
source |
: AC2
|
|
7)
|
chain |
P |
residue |
43 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE SO4 P 300
|
source |
: AC2
|
|
8)
|
chain |
P |
residue |
71 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE SO4 P 300
|
source |
: AC2
|
|
9)
|
chain |
P |
residue |
72 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE SO4 P 300
|
source |
: AC2
|
|
10)
|
chain |
P |
residue |
64 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE SO4 P 301
|
source |
: AC3
|
|
11)
|
chain |
P |
residue |
66 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE SO4 P 301
|
source |
: AC3
|
|
12)
|
chain |
P |
residue |
67 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE SO4 P 301
|
source |
: AC3
|
|
13)
|
chain |
P |
residue |
74 |
type |
|
sequence |
W
|
description |
BINDING SITE FOR RESIDUE SO4 P 301
|
source |
: AC3
|
|
14)
|
chain |
P |
residue |
75 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE SO4 P 301
|
source |
: AC3
|
|
15)
|
chain |
P |
residue |
209 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE SO4 P 301
|
source |
: AC3
|
|
16)
|
chain |
P |
residue |
14 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE BME P 314
|
source |
: AC4
|
|
17)
|
chain |
P |
residue |
28 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE BME P 314
|
source |
: AC4
|
|
18)
|
chain |
P |
residue |
73 |
type |
catalytic |
sequence |
E
|
description |
72
|
source |
MCSA : MCSA1
|
|
19)
|
chain |
P |
residue |
92 |
type |
catalytic |
sequence |
H
|
description |
72
|
source |
MCSA : MCSA1
|
|
20)
|
chain |
P |
residue |
94 |
type |
catalytic |
sequence |
H
|
description |
72
|
source |
MCSA : MCSA1
|
|
21)
|
chain |
P |
residue |
113 |
type |
catalytic |
sequence |
Y
|
description |
72
|
source |
MCSA : MCSA1
|
|
22)
|
chain |
P |
residue |
155 |
type |
catalytic |
sequence |
H
|
description |
72
|
source |
MCSA : MCSA1
|
|
23)
|
chain |
P |
residue |
209 |
type |
catalytic |
sequence |
Y
|
description |
72
|
source |
MCSA : MCSA1
|
|
24)
|
chain |
P |
residue |
73 |
type |
ACT_SITE |
sequence |
E
|
description |
Proton donor/acceptor => ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
25)
|
chain |
P |
residue |
28 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
26)
|
chain |
P |
residue |
43 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
27)
|
chain |
P |
residue |
71 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
28)
|
chain |
P |
residue |
73 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
29)
|
chain |
P |
residue |
92 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
30)
|
chain |
P |
residue |
94 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
31)
|
chain |
P |
residue |
155 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
32)
|
chain |
P |
residue |
113 |
type |
SITE |
sequence |
Y
|
description |
Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269|PubMed:10821675
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
33)
|
chain |
P |
residue |
131 |
type |
SITE |
sequence |
F
|
description |
Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269|PubMed:10821675
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
34)
|
chain |
P |
residue |
209 |
type |
SITE |
sequence |
Y
|
description |
Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269|PubMed:10821675
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
|
|