|
|
1)
|
chain |
C |
residue |
54 |
type |
|
sequence |
R
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
2)
|
chain |
C |
residue |
55 |
type |
|
sequence |
T
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
3)
|
chain |
C |
residue |
105 |
type |
|
sequence |
R
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
4)
|
chain |
C |
residue |
134 |
type |
|
sequence |
H
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
5)
|
chain |
C |
residue |
137 |
type |
|
sequence |
Q
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
6)
|
chain |
C |
residue |
167 |
type |
|
sequence |
R
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
7)
|
chain |
C |
residue |
229 |
type |
|
sequence |
R
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
8)
|
chain |
C |
residue |
231 |
type |
|
sequence |
Q
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
9)
|
chain |
C |
residue |
266 |
type |
|
sequence |
P
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
10)
|
chain |
C |
residue |
267 |
type |
|
sequence |
L
|
description |
BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
|
source |
: PMC
|
|
11)
|
chain |
C |
residue |
55 |
type |
catalytic |
sequence |
T
|
description |
405
|
source |
MCSA : MCSA2
|
|
12)
|
chain |
C |
residue |
56 |
type |
catalytic |
sequence |
R
|
description |
405
|
source |
MCSA : MCSA2
|
|
13)
|
chain |
C |
residue |
85 |
type |
catalytic |
sequence |
G
|
description |
405
|
source |
MCSA : MCSA2
|
|
14)
|
chain |
C |
residue |
106 |
type |
catalytic |
sequence |
H
|
description |
405
|
source |
MCSA : MCSA2
|
|
15)
|
chain |
C |
residue |
135 |
type |
catalytic |
sequence |
P
|
description |
405
|
source |
MCSA : MCSA2
|
|
16)
|
chain |
C |
residue |
106 |
type |
BINDING |
sequence |
H
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
C |
residue |
135 |
type |
BINDING |
sequence |
P
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
18)
|
chain |
C |
residue |
138 |
type |
BINDING |
sequence |
T
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
19)
|
chain |
C |
residue |
268 |
type |
BINDING |
sequence |
P
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
20)
|
chain |
C |
residue |
269 |
type |
BINDING |
sequence |
R
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
21)
|
chain |
C |
residue |
56 |
type |
BINDING |
sequence |
R
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
22)
|
chain |
C |
residue |
85 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
23)
|
chain |
C |
residue |
168 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
24)
|
chain |
C |
residue |
230 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
|
source |
Swiss-Prot : SWS_FT_FI2
|
|