|
|
1)
|
chain |
A |
residue |
42 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
81 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
82 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
84 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
119 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
120 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
121 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
182 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
183 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
188 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE SXC A 215
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
42 |
type |
catalytic |
sequence |
S
|
description |
631
|
source |
MCSA : MCSA1
|
|
12)
|
chain |
A |
residue |
120 |
type |
catalytic |
sequence |
S
|
description |
631
|
source |
MCSA : MCSA1
|
|
13)
|
chain |
A |
residue |
121 |
type |
catalytic |
sequence |
Q
|
description |
631
|
source |
MCSA : MCSA1
|
|
14)
|
chain |
A |
residue |
175 |
type |
catalytic |
sequence |
D
|
description |
631
|
source |
MCSA : MCSA1
|
|
15)
|
chain |
A |
residue |
188 |
type |
catalytic |
sequence |
H
|
description |
631
|
source |
MCSA : MCSA1
|
|
16)
|
chain |
A |
residue |
110-122 |
type |
prosite |
sequence |
PDATLIAGGYSQG
|
description |
CUTINASE_1 Cutinase, serine active site. PdAtLIaGGYSQG
|
source |
prosite : PS00155
|
|
17)
|
chain |
A |
residue |
171-188 |
type |
prosite |
sequence |
CKTGDLVCTGSLIVAAPH
|
description |
CUTINASE_2 Cutinase, aspartate and histidine active sites. CktgDlVCtGSliVaapH
|
source |
prosite : PS00931
|
|
18)
|
chain |
A |
residue |
120 |
type |
ACT_SITE |
sequence |
S
|
description |
Nucleophile => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
19)
|
chain |
A |
residue |
175 |
type |
ACT_SITE |
sequence |
D
|
description |
ACT_SITE => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
20)
|
chain |
A |
residue |
188 |
type |
ACT_SITE |
sequence |
H
|
description |
Proton donor/acceptor => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
A |
residue |
42 |
type |
SITE |
sequence |
S
|
description |
Transition state stabilizer => ECO:0000269|PubMed:1560844, ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:8555209, ECO:0000269|PubMed:9041628, ECO:0007744|PDB:1AGY, ECO:0007744|PDB:1FFE, ECO:0007744|PDB:1OXM, ECO:0007744|PDB:2CUT
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
22)
|
chain |
A |
residue |
121 |
type |
SITE |
sequence |
Q
|
description |
Transition state stabilizer => ECO:0000269|PubMed:1560844, ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:9041628, ECO:0007744|PDB:1AGY, ECO:0007744|PDB:1OXM, ECO:0007744|PDB:2CUT
|
source |
Swiss-Prot : SWS_FT_FI5
|
|