eF-site ID 2gjs-A
PDB Code 2gjs
Chain A

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Title The crystal structure of human RRAD in complex with GDP
Classification SIGNALING PROTEIN
Compound GTP-binding protein RAD
Source Homo sapiens (Human) (RAD_HUMAN)
Sequence A:  VYKVLLLGAPGVGKSALARIFGGVGHTYDRSIVVDGEEAS
LMVYDIWLPGHCMAMGDAYVIVYSVTDKGSFEKASELRVQ
LRRARQDVPIILVGNKSDLVRSREVSVDEGRACAVVFDCK
FIETSAALHHNVQALFEGVVRQIRLRRDSK
Description


Functional site

1) chain A
residue 105
type
sequence S
description BINDING SITE FOR RESIDUE MG A 1
source : AC1

2) chain A
residue 101
type
sequence G
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

3) chain A
residue 102
type
sequence V
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

4) chain A
residue 103
type
sequence G
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

5) chain A
residue 104
type
sequence K
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

6) chain A
residue 105
type
sequence S
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

7) chain A
residue 106
type
sequence A
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

8) chain A
residue 203
type
sequence N
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

9) chain A
residue 204
type
sequence K
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

10) chain A
residue 206
type
sequence D
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

11) chain A
residue 207
type
sequence L
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

12) chain A
residue 233
type
sequence S
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

13) chain A
residue 234
type
sequence A
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

14) chain A
residue 235
type
sequence A
description BINDING SITE FOR RESIDUE GDP A 1184
source : AC3

15) chain A
residue 100
type BINDING
sequence P
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 205
type BINDING
sequence S
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1


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