|
|
1)
|
chain |
A |
residue |
334 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE DTD B 505
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
337 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE DTD B 505
|
source |
: AC1
|
|
3)
|
chain |
B |
residue |
396 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE DTD B 505
|
source |
: AC1
|
|
4)
|
chain |
B |
residue |
399 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE DTD B 505
|
source |
: AC1
|
|
5)
|
chain |
B |
residue |
401 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE DTD B 505
|
source |
: AC1
|
|
6)
|
chain |
B |
residue |
469 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE DTD B 505
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
231 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE DTD A 506
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
232 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE DTD A 506
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
278 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE DTD A 506
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
290 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE DTD A 506
|
source |
: AC2
|
|
11)
|
chain |
A |
residue |
294 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE DTD A 506
|
source |
: AC2
|
|
12)
|
chain |
A |
residue |
260 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
13)
|
chain |
A |
residue |
317 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
14)
|
chain |
A |
residue |
318 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
15)
|
chain |
A |
residue |
358 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
16)
|
chain |
A |
residue |
360 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
17)
|
chain |
B |
residue |
411 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
18)
|
chain |
B |
residue |
412 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
19)
|
chain |
B |
residue |
413 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
20)
|
chain |
B |
residue |
415 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
21)
|
chain |
B |
residue |
420 |
type |
|
sequence |
W
|
description |
BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE
|
source |
: AC3
|
|
22)
|
chain |
A |
residue |
258 |
type |
catalytic |
sequence |
R
|
description |
818
|
source |
MCSA : MCSA1
|
|
23)
|
chain |
A |
residue |
317 |
type |
catalytic |
sequence |
H
|
description |
818
|
source |
MCSA : MCSA1
|
|
24)
|
chain |
A |
residue |
318 |
type |
catalytic |
sequence |
G
|
description |
818
|
source |
MCSA : MCSA1
|
|
25)
|
chain |
A |
residue |
360 |
type |
catalytic |
sequence |
C
|
description |
818
|
source |
MCSA : MCSA1
|
|
26)
|
chain |
A |
residue |
304-318 |
type |
prosite |
sequence |
HSNMDCFICCILSHG
|
description |
CASPASE_HIS Caspase family histidine active site. HsnmdCfiCcILSHG
|
source |
prosite : PS01121
|
|
27)
|
chain |
A |
residue |
351-362 |
type |
prosite |
sequence |
KPKVFFIQACQG
|
description |
CASPASE_CYS Caspase family cysteine active site. KPKVFFIQACQG
|
source |
prosite : PS01122
|
|
28)
|
chain |
A |
residue |
360 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine; by CDK1 => ECO:0000269|PubMed:20937773
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
29)
|
chain |
B |
residue |
413 |
type |
MOD_RES |
sequence |
R
|
description |
(Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
30)
|
chain |
A |
residue |
374 |
type |
SITE |
sequence |
D
|
description |
Cleavage; by CASP6 => ECO:0000269|PubMed:22858542
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
31)
|
chain |
A |
residue |
224 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:O89110
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
32)
|
chain |
A |
residue |
334 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:15592455
|
source |
Swiss-Prot : SWS_FT_FI6
|
|