eF-site ID 1l9x-B
PDB Code 1l9x
Chain B

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Title Structure of gamma-Glutamyl Hydrolase
Classification HYDROLASE
Compound gamma-glutamyl hydrolase
Source Homo sapiens (Human) (GGH_HUMAN)
Sequence B:  GLVPRGAKKPIIGILMQKCRNKVMKNYGRYYIAASYVKYL
ESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRR
SDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLI
SGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLS
LAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGK
IEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNA
VKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPIY
TGNISSFQQCYIFD
Description (1)  gamma-glutamyl hydrolase (E.C.3.4.19.9)


Functional site

1) chain B
residue 73
type
sequence G
description BINDING SITE FOR RESIDUE BME B 1002
source : AC2

2) chain B
residue 74
type
sequence G
description BINDING SITE FOR RESIDUE BME B 1002
source : AC2

3) chain B
residue 110
type
sequence C
description BINDING SITE FOR RESIDUE BME B 1002
source : AC2

4) chain B
residue 111
type
sequence L
description BINDING SITE FOR RESIDUE BME B 1002
source : AC2

5) chain B
residue 170
type
sequence F
description BINDING SITE FOR RESIDUE BME B 1002
source : AC2

6) chain B
residue 220
type
sequence H
description BINDING SITE FOR RESIDUE BME B 1002
source : AC2

7) chain B
residue 118
type
sequence L
description BINDING SITE FOR RESIDUE BME B 1003
source : AC3

8) chain B
residue 124
type
sequence C
description BINDING SITE FOR RESIDUE BME B 1003
source : AC3

9) chain B
residue 126
type
sequence L
description BINDING SITE FOR RESIDUE BME B 1003
source : AC3

10) chain B
residue 110
type catalytic
sequence C
description 747
source MCSA : MCSA2

11) chain B
residue 220
type catalytic
sequence H
description 747
source MCSA : MCSA2

12) chain B
residue 222
type catalytic
sequence E
description 747
source MCSA : MCSA2

13) chain B
residue 110
type ACT_SITE
sequence C
description Nucleophile
source Swiss-Prot : SWS_FT_FI1

14) chain B
residue 283
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:11953431
source Swiss-Prot : SWS_FT_FI5

15) chain B
residue 139
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11953431
source Swiss-Prot : SWS_FT_FI4

16) chain B
residue 179
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11953431
source Swiss-Prot : SWS_FT_FI4

17) chain B
residue 220
type ACT_SITE
sequence H
description Proton donor
source Swiss-Prot : SWS_FT_FI2

18) chain B
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI3


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