eF-site ID 1fdy-C
PDB Code 1fdy
Chain C

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Title N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE
Classification LYASE
Compound N-ACETYLNEURAMINATE LYASE
Source Escherichia coli (strain K12) (NANA_ECOLI)
Sequence C:  NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLY
VGGSTGEAFVQSLSEREQVLEIVAEEGKGKIKLIAHVGCV
TTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYR
AIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA
LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD
GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI
DLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLP
ELKALAQQLMQ
Description


Functional site

1) chain C
residue 43
type
sequence Y
description BINDING SITE FOR RESIDUE 3PY C 806
source : AC3

2) chain C
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE 3PY C 806
source : AC3

3) chain C
residue 47
type
sequence S
description BINDING SITE FOR RESIDUE 3PY C 806
source : AC3

4) chain C
residue 48
type
sequence T
description BINDING SITE FOR RESIDUE 3PY C 806
source : AC3

5) chain C
residue 137
type
sequence Y
description BINDING SITE FOR RESIDUE 3PY C 806
source : AC3

6) chain C
residue 165
type
sequence K
description BINDING SITE FOR RESIDUE 3PY C 806
source : AC3

7) chain C
residue 137
type catalytic
sequence Y
description 553
source MCSA : MCSA3

8) chain C
residue 165
type catalytic
sequence K
description 553
source MCSA : MCSA3

9) chain C
residue 167
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL
source Swiss-Prot : SWS_FT_FI4

10) chain C
residue 189
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL
source Swiss-Prot : SWS_FT_FI4

11) chain C
residue 191
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL
source Swiss-Prot : SWS_FT_FI4

12) chain C
residue 192
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL
source Swiss-Prot : SWS_FT_FI4

13) chain C
residue 208
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL
source Swiss-Prot : SWS_FT_FI4

14) chain C
residue 47
type SITE
sequence S
description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460
source Swiss-Prot : SWS_FT_FI5

15) chain C
residue 110
type SITE
sequence Y
description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460
source Swiss-Prot : SWS_FT_FI5

16) chain C
residue 165
type ACT_SITE
sequence K
description Schiff-base intermediate with substrate => ECO:0000269|PubMed:12711733, ECO:0000269|PubMed:19923724, ECO:0000269|PubMed:24521460, ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:8081752
source Swiss-Prot : SWS_FT_FI2

17) chain C
residue 47
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:12711733, ECO:0007744|PDB:1FDY, ECO:0007744|PDB:1FDZ, ECO:0007744|PDB:1HL2
source Swiss-Prot : SWS_FT_FI3

18) chain C
residue 48
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:12711733, ECO:0007744|PDB:1FDY, ECO:0007744|PDB:1FDZ, ECO:0007744|PDB:1HL2
source Swiss-Prot : SWS_FT_FI3

19) chain C
residue 137
type ACT_SITE
sequence Y
description Proton donor => ECO:0000305|PubMed:24521460
source Swiss-Prot : SWS_FT_FI1


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