|
|
1)
|
chain |
C |
residue |
134 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000250|UniProtKB:P09601
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
2)
|
chain |
C |
residue |
183 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P09601
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
3)
|
chain |
A |
residue |
134 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000250|UniProtKB:P09601
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
4)
|
chain |
A |
residue |
183 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P09601
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
5)
|
chain |
B |
residue |
134 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000250|UniProtKB:P09601
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
6)
|
chain |
B |
residue |
183 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P09601
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
7)
|
chain |
C |
residue |
129-139 |
type |
prosite |
sequence |
LVAHAYTRYLG
|
description |
HEME_OXYGENASE Heme oxygenase signature. LVAHAYTRYLG
|
source |
prosite : PS00593
|
|
8)
|
chain |
C |
residue |
140 |
type |
SITE |
sequence |
D
|
description |
Important for catalytic activity => ECO:0000250|UniProtKB:P09601
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
9)
|
chain |
A |
residue |
140 |
type |
SITE |
sequence |
D
|
description |
Important for catalytic activity => ECO:0000250|UniProtKB:P09601
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
10)
|
chain |
B |
residue |
140 |
type |
SITE |
sequence |
D
|
description |
Important for catalytic activity => ECO:0000250|UniProtKB:P09601
|
source |
Swiss-Prot : SWS_FT_FI4
|
|