eF-site ID 1ffa-A
PDB Code 1ffa
Chain A

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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 Fusarium solani subsp. pisi (Nectria haematococca) (CUTI1_FUSSO)
Sequence A:  RTTRDDLINGNSASCRDVIFIYARGSTETGNLGTLGPSIA
SNLESAFGKDGVWIQGVGGAYRATLGDAALPRGTSSAAIR
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


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