|
eF-site ID
|
4u2c-A |
PDB Code
|
4u2c |
Chain
|
A |
|
click to enlarge
|
|
Title
|
Crystal structure of dienelactone hydrolase A-6 variant (S7T, A24V, Q35H, F38L, Q110L, C123S, Y145C, E199G and S208G) at 1.95 A resolution |
Classification
|
HYDROLASE |
Compound
|
Carboxymethylenebutenolidase |
Source
|
(CLCD_PSESB) |
|
Sequence
|
A: |
MLTEGITIQSYDGHTFGALVGSPVKAPAPVIVIAHEILGV
NAFMRETVSWLVDQGYAAVCPDLYARQAPGTALDPQDEAQ
REQAYKLWQAFDMEAGVGDLEAAIRYARHLPYSNGKVGLV
GYSLGGALAFLVAAKGYVDRAVGYXGVGLEKQLNKVPEVK
HPALFHMGGQDHFVPAPSRQLITEGFGANPLLQVHWYEGA
GHSFARTGSSGYVASAAALANERTLDFLAPLQS
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
1 |
type |
|
sequence |
M
|
description |
binding site for residue SO4 A 301
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
72 |
type |
|
sequence |
A
|
description |
binding site for residue SO4 A 301
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
99-127 |
type |
prosite |
sequence |
DLEAAIRYARHLPYSNGKVGLVGYSLGGA
|
description |
ADH_SHORT Short-chain dehydrogenases/reductases family signature. DleaairyarHlpYSNGKVGLvGYSlGGA
|
source |
prosite : PS00061
|
|
4)
|
chain |
A |
residue |
36 |
type |
catalytic |
sequence |
E
|
description |
492
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
A |
residue |
37 |
type |
catalytic |
sequence |
I
|
description |
492
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
A |
residue |
85 |
type |
catalytic |
sequence |
Y
|
description |
492
|
source |
MCSA : MCSA1
|
|
7)
|
chain |
A |
residue |
123 |
type |
catalytic |
sequence |
S
|
description |
492
|
source |
MCSA : MCSA1
|
|
8)
|
chain |
A |
residue |
124 |
type |
catalytic |
sequence |
L
|
description |
492
|
source |
MCSA : MCSA1
|
|
9)
|
chain |
A |
residue |
171 |
type |
catalytic |
sequence |
D
|
description |
492
|
source |
MCSA : MCSA1
|
|
10)
|
chain |
A |
residue |
202 |
type |
catalytic |
sequence |
H
|
description |
492
|
source |
MCSA : MCSA1
|
|
11)
|
chain |
A |
residue |
123 |
type |
ACT_SITE |
sequence |
S
|
description |
ACT_SITE => ECO:0000269|PubMed:3221394
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
12)
|
chain |
A |
residue |
171 |
type |
ACT_SITE |
sequence |
D
|
description |
ACT_SITE => ECO:0000269|PubMed:3221394
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
13)
|
chain |
A |
residue |
202 |
type |
ACT_SITE |
sequence |
H
|
description |
ACT_SITE => ECO:0000269|PubMed:3221394
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
|
|