|
eF-site ID
|
1tim-AB |
PDB Code
|
1tim |
Chain
|
A, B |
|
click to enlarge
|
|
Title
|
STRUCTURE OF TRIOSE PHOSPHATE ISOMERASE FROM CHICKEN MUSCLE |
Classification
|
ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) |
Compound
|
TRIOSEPHOSPHATE ISOMERASE |
Source
|
Gallus gallus (Chicken) (TPIS_CHICK) |
|
Sequence
|
A: |
APRKFFVGGNWKMNGKRKSLGELIHTLDGAKLSADTEVVC
GAPSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPA
MIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGL
GVIACIGEKLDEREAGITEKVVFQETKAIADNVKDWSKVV
LAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVSDAVA
VQSRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFV
DIINAKH
|
B: |
APRKFFVGGNWKMNGKRKSLGELIHTLDGAKLSADTEVVC
GAPSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPA
MIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGL
GVIACIGEKLDEREAGITEKVVFQETKAIADNVKDWSKVV
LAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVSDAVA
VQSRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFV
DIINAKH
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
11 |
type |
catalytic |
sequence |
N
|
description |
324
|
source |
MCSA : MCSA1
|
|
2)
|
chain |
A |
residue |
13 |
type |
catalytic |
sequence |
K
|
description |
324
|
source |
MCSA : MCSA1
|
|
3)
|
chain |
A |
residue |
95 |
type |
catalytic |
sequence |
H
|
description |
324
|
source |
MCSA : MCSA1
|
|
4)
|
chain |
A |
residue |
97 |
type |
catalytic |
sequence |
E
|
description |
324
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
A |
residue |
165 |
type |
catalytic |
sequence |
E
|
description |
324
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
A |
residue |
171 |
type |
catalytic |
sequence |
G
|
description |
324
|
source |
MCSA : MCSA1
|
|
7)
|
chain |
A |
residue |
211 |
type |
catalytic |
sequence |
S
|
description |
324
|
source |
MCSA : MCSA1
|
|
8)
|
chain |
B |
residue |
11 |
type |
catalytic |
sequence |
N
|
description |
324
|
source |
MCSA : MCSA2
|
|
9)
|
chain |
B |
residue |
13 |
type |
catalytic |
sequence |
K
|
description |
324
|
source |
MCSA : MCSA2
|
|
10)
|
chain |
B |
residue |
95 |
type |
catalytic |
sequence |
H
|
description |
324
|
source |
MCSA : MCSA2
|
|
11)
|
chain |
B |
residue |
97 |
type |
catalytic |
sequence |
E
|
description |
324
|
source |
MCSA : MCSA2
|
|
12)
|
chain |
B |
residue |
165 |
type |
catalytic |
sequence |
E
|
description |
324
|
source |
MCSA : MCSA2
|
|
13)
|
chain |
B |
residue |
171 |
type |
catalytic |
sequence |
G
|
description |
324
|
source |
MCSA : MCSA2
|
|
14)
|
chain |
B |
residue |
212 |
type |
catalytic |
sequence |
V
|
description |
324
|
source |
MCSA : MCSA2
|
|
15)
|
chain |
A |
residue |
95 |
type |
ACT_SITE |
sequence |
H
|
description |
Electrophile => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
B |
residue |
95 |
type |
ACT_SITE |
sequence |
H
|
description |
Electrophile => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
A |
residue |
165 |
type |
ACT_SITE |
sequence |
E
|
description |
Proton acceptor => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
B |
residue |
165 |
type |
ACT_SITE |
sequence |
E
|
description |
Proton acceptor => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
A |
residue |
11 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
20)
|
chain |
A |
residue |
13 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
B |
residue |
11 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
22)
|
chain |
B |
residue |
13 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
23)
|
chain |
A |
residue |
163-173 |
type |
prosite |
sequence |
AYEPVWAIGTG
|
description |
TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
|
source |
prosite : PS00171
|
|
|
|