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PDBsum entry 4xhg
Go to PDB code:
Transferase
PDB id
4xhg
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Contents
Protein chain
357 a.a.
Ligands
ADP
FMT
Waters
×285
PDB id:
4xhg
Links
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ProSAT
Name:
Transferase
Title:
Structure of c. Glabrata hrr25 bound to adp (formate condition)
Structure:
Similar to uniprot|p29295 saccharomyces cerevisiae ypl204w hrr25. Chain: a. Fragment: unp residues 1-403. Engineered: yes. Mutation: yes
Source:
Candida glabrata. Organism_taxid: 5478. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.15Å
R-factor:
0.176
R-free:
0.216
Authors:
Q.Ye,K.D.Corbett
Key ref:
Q.Ye et al. (2016). Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator.
Embo J
,
35
, 2139-2151.
PubMed id:
27491543
DOI:
10.15252/embj.201694082
Date:
05-Jan-15
Release date:
06-Jan-16
PROCHECK
Headers
References
Protein chain
?
Q6FS46
(Q6FS46_CANGA) - Candida glabrata strain CBS138 chromosome H complete sequence from Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138)
Seq:
Struc:
495 a.a.
357 a.a.
*
Key:
PfamA domain
Secondary structure
*
PDB and UniProt seqs differ at 1 residue position (black cross)
Enzyme reactions
Enzyme class:
E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
1.
L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H
+
2.
L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H
+
L-seryl-[protein]
+
ATP
=
O-phospho-L-seryl-[protein]
Bound ligand (Het Group name =
ADP
)
corresponds exactly
+
ADP
+
H(+)
L-threonyl-[protein]
+
ATP
=
O-phospho-L-threonyl-[protein]
Bound ligand (Het Group name =
ADP
)
corresponds exactly
+
ADP
+
H(+)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
reference
DOI no:
10.15252/embj.201694082
Embo J
35
:2139-2151 (2016)
PubMed id:
27491543
Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator.
Q.Ye,
S.N.Ur,
T.Y.Su,
K.D.Corbett.
ABSTRACT
No abstract given.
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