|
|
1)
|
chain |
A |
residue |
70 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE PB A1319
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
96 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE PB A1319
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
71 |
type |
catalytic |
sequence |
G
|
description |
510
|
source |
MCSA : MCSA1
|
|
4)
|
chain |
A |
residue |
97 |
type |
catalytic |
sequence |
T
|
description |
510
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
A |
residue |
172 |
type |
catalytic |
sequence |
V
|
description |
510
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
A |
residue |
211 |
type |
catalytic |
sequence |
L
|
description |
510
|
source |
MCSA : MCSA1
|
|
7)
|
chain |
A |
residue |
213 |
type |
catalytic |
sequence |
V
|
description |
510
|
source |
MCSA : MCSA1
|
|
8)
|
chain |
A |
residue |
284 |
type |
catalytic |
sequence |
Y
|
description |
510
|
source |
MCSA : MCSA1
|
|
9)
|
chain |
A |
residue |
309 |
type |
catalytic |
sequence |
H
|
description |
510
|
source |
MCSA : MCSA1
|
|
10)
|
chain |
A |
residue |
310 |
type |
catalytic |
sequence |
C
|
description |
510
|
source |
MCSA : MCSA1
|
|
11)
|
chain |
A |
residue |
89-98 |
type |
prosite |
sequence |
PDILCLQETK
|
description |
AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQETK
|
source |
prosite : PS00726
|
|
12)
|
chain |
A |
residue |
251-267 |
type |
prosite |
sequence |
DSFRHLYPNTPYAYTFW
|
description |
AP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DSFRHlypntpyaYTFW
|
source |
prosite : PS00727
|
|
13)
|
chain |
A |
residue |
277-288 |
type |
prosite |
sequence |
NVGWRLDYFLLS
|
description |
AP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NvGwRLDYfLlS
|
source |
prosite : PS00728
|
|
14)
|
chain |
A |
residue |
172 |
type |
ACT_SITE |
sequence |
V
|
description |
ACT_SITE => ECO:0000269|PubMed:15380100
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
15)
|
chain |
A |
residue |
55 |
type |
MOD_RES |
sequence |
P
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI11
|
|
16)
|
chain |
A |
residue |
66 |
type |
MOD_RES |
sequence |
S
|
description |
S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694
|
source |
Swiss-Prot : SWS_FT_FI12
|
|
17)
|
chain |
A |
residue |
94 |
type |
MOD_RES |
sequence |
L
|
description |
S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694
|
source |
Swiss-Prot : SWS_FT_FI12
|
|
18)
|
chain |
A |
residue |
198 |
type |
MOD_RES |
sequence |
G
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI13
|
|
19)
|
chain |
A |
residue |
234 |
type |
MOD_RES |
sequence |
P
|
description |
Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352
|
source |
Swiss-Prot : SWS_FT_FI14
|
|
20)
|
chain |
A |
residue |
311 |
type |
MOD_RES |
sequence |
P
|
description |
S-nitrosocysteine => ECO:0000269|PubMed:17403694
|
source |
Swiss-Prot : SWS_FT_FI15
|
|
21)
|
chain |
A |
residue |
211 |
type |
ACT_SITE |
sequence |
L
|
description |
Proton donor/acceptor => ECO:0000269|PubMed:9351835, ECO:0007744|PDB:1BIX
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
22)
|
chain |
A |
residue |
310 |
type |
ACT_SITE |
sequence |
C
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
23)
|
chain |
A |
residue |
69 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00764
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
24)
|
chain |
A |
residue |
97 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00764
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
25)
|
chain |
A |
residue |
211 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00764
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
26)
|
chain |
A |
residue |
213 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00764
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
27)
|
chain |
A |
residue |
309 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00764
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
28)
|
chain |
A |
residue |
310 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00764
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
29)
|
chain |
A |
residue |
213 |
type |
SITE |
sequence |
V
|
description |
Transition state stabilizer => ECO:0000269|PubMed:8932375
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
30)
|
chain |
A |
residue |
284 |
type |
SITE |
sequence |
Y
|
description |
Important for catalytic activity => ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:9804799
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
31)
|
chain |
A |
residue |
310 |
type |
SITE |
sequence |
C
|
description |
Interaction with DNA substrate
|
source |
Swiss-Prot : SWS_FT_FI8
|
|