|
|
eF-site ID
|
1ffd-A |
|
PDB Code
|
1ffd |
|
Chain
|
A |
|
click to enlarge
|
|
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Title
|
CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATION OF THE OXYANION TRANSITION STATE |
|
Classification
|
HYDROLASE (SERINE ESTERASE) |
|
Compound
|
CUTINASE |
|
Source
|
(CUTI1_FUSSO) |
|
|
Sequence
|
A: |
RTTRDDLINGNSASCRDVIFIYARGSTETGNLGTLGPSIA
SNLESAFGKDGVWIQGVGGAYRATLGDWALPRGTSSAAIR
EMLGLFQQANTKCPDATLIAGGYSQGAALAAASIEDLDSA
IRDKIAGTVLFGYTKNLQNRGRIPNYPADRTKVFCNTGDL
VCTGSLIVAAPHLAYGPDARGPAPEFLIEKVRAVRGS
|
|
|
Description
|
|
Functional site
|
|
|
1)
|
chain |
A |
| residue |
120 |
| type |
|
| sequence |
S
|
| description |
|
| source |
: CAT
|
|
|
2)
|
chain |
A |
| residue |
188 |
| type |
|
| sequence |
H
|
| description |
|
| source |
: CAT
|
|
|
3)
|
chain |
A |
| residue |
175 |
| type |
|
| sequence |
D
|
| description |
|
| 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 |
CNTGDLVCTGSLIVAAPH
|
| description |
CUTINASE_2 Cutinase, aspartate and histidine active sites. CntgDlVCtGSliVaapH
|
| 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
|
|
|
|