eF-site ID 1e55-B
PDB Code 1e55
Chain B

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Title Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) beta-glucosidase ZMGluE191D in complex with the competitive inhibitor dhurrin
Classification HYDROLASE
Compound BETA-GLUCOSIDASE
Source (BGLC_MAIZE)
Sequence B:  MLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGES
NWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEMG
MDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLLLE
NGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTYF
AKVCFDNFGDKVKNWLTFNDPQTFTSFSYGTGVFAPGRCS
PGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKR
DDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFLE
PVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGLN
YYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPIG
PPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGD
VDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNV
QGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKES
AKWLKEFNTA
Description


Functional site

1) chain B
residue 457
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49
source Swiss-Prot : SWS_FT_FI6

2) chain B
residue 464
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49
source Swiss-Prot : SWS_FT_FI6

3) chain B
residue 191
type ACT_SITE
sequence D
description Proton donor => ECO:0000250|UniProtKB:Q7XKV4
source Swiss-Prot : SWS_FT_FI1

4) chain B
residue 406
type ACT_SITE
sequence E
description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4
source Swiss-Prot : SWS_FT_FI2

5) chain B
residue 38
type BINDING
sequence Q
description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49
source Swiss-Prot : SWS_FT_FI3

6) chain B
residue 142
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56
source Swiss-Prot : SWS_FT_FI4

7) chain B
residue 190
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56
source Swiss-Prot : SWS_FT_FI4

8) chain B
residue 333
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56
source Swiss-Prot : SWS_FT_FI4

9) chain B
residue 473
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56
source Swiss-Prot : SWS_FT_FI4

10) chain B
residue 406
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:Q9SPP9
source Swiss-Prot : SWS_FT_FI5


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