|
eF-site ID
|
1cua-A |
PDB Code
|
1cua |
Chain
|
A |
|
click to enlarge
|
|
Title
|
CUTINASE, N172K MUTANT |
Classification
|
HYDROLASE (SERINE ESTERASE) |
Compound
|
CUTINASE |
Source
|
Fusarium solani subsp. pisi (Nectria haematococca) (CUTI1_FUSSO) |
|
Sequence
|
A: |
RTTRDDLINGNSASCADVIFIYARGSTETGNLGTLGPSIA
SNLESAFGKDGVWIQGVGGAYRATLGDNALPRGTSSAAIR
EMLGLFQQANTKCPDATLIAGGYSQGAALAAASIEDLDSA
IRDKIAGTVLFGYTKNLQNRGRIPNYPADRTKVFCKTGDL
VCTGSLIVAAPHLAYGPDARGPAPEFLIEKVRAVRGS
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
120 |
type |
|
sequence |
S
|
description |
CATALYTIC TRIAD
|
source |
: CAT
|
|
2)
|
chain |
A |
residue |
188 |
type |
|
sequence |
H
|
description |
CATALYTIC TRIAD
|
source |
: CAT
|
|
3)
|
chain |
A |
residue |
175 |
type |
|
sequence |
D
|
description |
CATALYTIC TRIAD
|
source |
: CAT
|
|
4)
|
chain |
A |
residue |
42 |
type |
catalytic |
sequence |
S
|
description |
631
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
A |
residue |
120 |
type |
catalytic |
sequence |
S
|
description |
631
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
A |
residue |
121 |
type |
catalytic |
sequence |
Q
|
description |
631
|
source |
MCSA : MCSA1
|
|
7)
|
chain |
A |
residue |
175 |
type |
catalytic |
sequence |
D
|
description |
631
|
source |
MCSA : MCSA1
|
|
8)
|
chain |
A |
residue |
188 |
type |
catalytic |
sequence |
H
|
description |
631
|
source |
MCSA : MCSA1
|
|
9)
|
chain |
A |
residue |
110-122 |
type |
prosite |
sequence |
PDATLIAGGYSQG
|
description |
CUTINASE_1 Cutinase, serine active site. PdAtLIaGGYSQG
|
source |
prosite : PS00155
|
|
10)
|
chain |
A |
residue |
171-188 |
type |
prosite |
sequence |
CKTGDLVCTGSLIVAAPH
|
description |
CUTINASE_2 Cutinase, aspartate and histidine active sites. CktgDlVCtGSliVaapH
|
source |
prosite : PS00931
|
|
11)
|
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
|
|
12)
|
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
|
|
13)
|
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
|
|
14)
|
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
|
|
15)
|
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
|
|
|
|