|
|
1)
|
chain |
A |
residue |
19 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
55 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
60 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
63 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
72 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
101 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
102 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
103 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
111 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
113 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
121 |
type |
|
sequence |
W
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
125 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
13)
|
chain |
A |
residue |
126 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
14)
|
chain |
A |
residue |
164 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR CHAIN C OF CYCLOSPORIN C
|
source |
: AC1
|
|
15)
|
chain |
A |
residue |
56 |
type |
catalytic |
sequence |
I
|
description |
189
|
source |
MCSA : MCSA1
|
|
16)
|
chain |
A |
residue |
61 |
type |
catalytic |
sequence |
M
|
description |
189
|
source |
MCSA : MCSA1
|
|
17)
|
chain |
A |
residue |
64 |
type |
catalytic |
sequence |
G
|
description |
189
|
source |
MCSA : MCSA1
|
|
18)
|
chain |
A |
residue |
103 |
type |
catalytic |
sequence |
A
|
description |
189
|
source |
MCSA : MCSA1
|
|
19)
|
chain |
A |
residue |
114 |
type |
catalytic |
sequence |
I
|
description |
189
|
source |
MCSA : MCSA1
|
|
20)
|
chain |
A |
residue |
123 |
type |
catalytic |
sequence |
D
|
description |
189
|
source |
MCSA : MCSA1
|
|
21)
|
chain |
A |
residue |
127 |
type |
catalytic |
sequence |
V
|
description |
189
|
source |
MCSA : MCSA1
|
|
22)
|
chain |
A |
residue |
48-65 |
type |
prosite |
sequence |
YKGSCFHRIIPGFMCQGG
|
description |
CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG
|
source |
prosite : PS00170
|
|
23)
|
chain |
A |
residue |
2 |
type |
MOD_RES |
sequence |
V
|
description |
N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
24)
|
chain |
A |
residue |
29 |
type |
CROSSLNK |
sequence |
V
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
25)
|
chain |
A |
residue |
83 |
type |
CROSSLNK |
sequence |
F
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI11
|
|
26)
|
chain |
A |
residue |
3 |
type |
MOD_RES |
sequence |
N
|
description |
N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
27)
|
chain |
A |
residue |
29 |
type |
MOD_RES |
sequence |
V
|
description |
N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
28)
|
chain |
A |
residue |
83 |
type |
MOD_RES |
sequence |
F
|
description |
N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
29)
|
chain |
A |
residue |
45 |
type |
MOD_RES |
sequence |
G
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
30)
|
chain |
A |
residue |
77 |
type |
MOD_RES |
sequence |
S
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
31)
|
chain |
A |
residue |
132 |
type |
MOD_RES |
sequence |
V
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
32)
|
chain |
A |
residue |
78 |
type |
MOD_RES |
sequence |
I
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
33)
|
chain |
A |
residue |
94 |
type |
MOD_RES |
sequence |
G
|
description |
Phosphothreonine => ECO:0007744|PubMed:20068231
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
34)
|
chain |
A |
residue |
126 |
type |
MOD_RES |
sequence |
H
|
description |
N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
35)
|
chain |
A |
residue |
134 |
type |
MOD_RES |
sequence |
E
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:P17742
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
36)
|
chain |
A |
residue |
109 |
type |
CARBOHYD |
sequence |
G
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI9
|
|