eF-site ID 1hu0-A
PDB Code 1hu0
Chain A

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Title CRYSTAL STRUCTURE OF AN HOGG1-DNA BOROHYDRIDE TRAPPED INTERMEDIATE COMPLEX
Classification HYDROLASE/DNA
Compound 5'-D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3'
Source Homo sapiens (Human) (1HU0)
Sequence A:  GSEGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWR
EQSPAHWSGVLADQVWTLTQTEEQLHCTVYRSQASRPTPD
ELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVR
LLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLI
QLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSAS
ARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVA
DCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGP
SPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQ
Description


Functional site

1) chain A
residue 42
type
sequence G
description BINDING SITE FOR RESIDUE OXG A 328
source : AC2

2) chain A
residue 45
type
sequence F
description BINDING SITE FOR RESIDUE OXG A 328
source : AC2

3) chain A
residue 144
type
sequence F
description BINDING SITE FOR RESIDUE OXG A 328
source : AC2

4) chain A
residue 249
type
sequence K
description BINDING SITE FOR RESIDUE OXG A 328
source : AC2

5) chain A
residue 266
type
sequence P
description BINDING SITE FOR RESIDUE OXG A 328
source : AC2

6) chain A
residue 268
type
sequence D
description BINDING SITE FOR RESIDUE OXG A 328
source : AC2

7) chain A
residue 315
type
sequence Q
description BINDING SITE FOR RESIDUE OXG A 328
source : AC2

8) chain A
residue 319
type
sequence F
description BINDING SITE FOR RESIDUE OXG A 328
source : AC2

9) chain A
residue 249
type catalytic
sequence K
description 185
source MCSA : MCSA1

10) chain A
residue 268
type catalytic
sequence D
description 185
source MCSA : MCSA1

11) chain A
residue 249
type ACT_SITE
sequence K
description Schiff-base intermediate with DNA => ECO:0000269|PubMed:9197244
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 149
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848
source Swiss-Prot : SWS_FT_FI2

13) chain A
residue 154
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 204
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848
source Swiss-Prot : SWS_FT_FI2

15) chain A
residue 270
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848
source Swiss-Prot : SWS_FT_FI2

16) chain A
residue 287
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848
source Swiss-Prot : SWS_FT_FI2

17) chain A
residue 266
type BINDING
sequence P
description
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 268
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI3

19) chain A
residue 315
type BINDING
sequence Q
description
source Swiss-Prot : SWS_FT_FI3

20) chain A
residue 319
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI3


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