|
|
1)
|
chain |
B |
residue |
362 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE CL B 2
|
source |
: AC2
|
|
2)
|
chain |
B |
residue |
461 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE CL B 2
|
source |
: AC2
|
|
3)
|
chain |
B |
residue |
462 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE CL B 2
|
source |
: AC2
|
|
4)
|
chain |
B |
residue |
524 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE CL B 2
|
source |
: AC2
|
|
5)
|
chain |
B |
residue |
331 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
6)
|
chain |
B |
residue |
363 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
7)
|
chain |
B |
residue |
432 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
8)
|
chain |
B |
residue |
433 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
9)
|
chain |
B |
residue |
434 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
10)
|
chain |
B |
residue |
435 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
11)
|
chain |
B |
residue |
436 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
12)
|
chain |
B |
residue |
437 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
13)
|
chain |
B |
residue |
464 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
14)
|
chain |
B |
residue |
465 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR
|
source |
: AC6
|
|
15)
|
chain |
B |
residue |
363 |
type |
catalytic |
sequence |
H
|
description |
238
|
source |
MCSA : MCSA2
|
|
16)
|
chain |
B |
residue |
432 |
type |
catalytic |
sequence |
S
|
description |
238
|
source |
MCSA : MCSA2
|
|
17)
|
chain |
B |
residue |
434 |
type |
catalytic |
sequence |
S
|
description |
238
|
source |
MCSA : MCSA2
|
|
18)
|
chain |
B |
residue |
457 |
type |
catalytic |
sequence |
H
|
description |
238
|
source |
MCSA : MCSA2
|
|
19)
|
chain |
B |
residue |
465 |
type |
catalytic |
sequence |
R
|
description |
238
|
source |
MCSA : MCSA2
|
|
20)
|
chain |
B |
residue |
466 |
type |
catalytic |
sequence |
R
|
description |
238
|
source |
MCSA : MCSA2
|
|
21)
|
chain |
B |
residue |
363 |
type |
ACT_SITE |
sequence |
H
|
description |
Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
22)
|
chain |
B |
residue |
432 |
type |
ACT_SITE |
sequence |
S
|
description |
Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
23)
|
chain |
B |
residue |
457 |
type |
ACT_SITE |
sequence |
H
|
description |
Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
24)
|
chain |
B |
residue |
556 |
type |
SITE |
sequence |
A
|
description |
Cleavage; by assemblin; Release site => ECO:0000255|HAMAP-Rule:MF_04008
|
source |
Swiss-Prot : SWS_FT_FI2
|
|