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

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Title Structure of gamma-Glutamyl Hydrolase
Classification HYDROLASE
Compound gamma-glutamyl hydrolase
Source Homo sapiens (Human) (GGH_HUMAN)
Sequence D:  GLVPRAKKPIIGILMQKCRNKVMKNYGRYYIAASYVKYLE
SAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRS
DYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLIS
GECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSL
AVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKI
EFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAV
KTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPIYT
GNISSFQQCYIFD
Description (1)  gamma-glutamyl hydrolase (E.C.3.4.19.9)


Functional site

1) chain D
residue 114
type
sequence E
description BINDING SITE FOR RESIDUE BME D 1006
source : AC6

2) chain D
residue 124
type
sequence C
description BINDING SITE FOR RESIDUE BME D 1006
source : AC6

3) chain D
residue 126
type
sequence L
description BINDING SITE FOR RESIDUE BME D 1006
source : AC6

4) chain D
residue 110
type catalytic
sequence C
description 747
source MCSA : MCSA4

5) chain D
residue 220
type catalytic
sequence H
description 747
source MCSA : MCSA4

6) chain D
residue 222
type catalytic
sequence E
description 747
source MCSA : MCSA4

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

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

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

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

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

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


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