Structure of PDB 6tp5 Chain A Binding Site BS03
Receptor Information
>6tp5 Chain A (length=370) Species:
9606
(Homo sapiens) [
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TLGPLTRLEGIKVGHERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEEC
RLIIHLAQMKGLQRSQILPTEEYEEQVSQLDLFRLLDQNRDGHLQLREVL
AQTRLGNGWWMTPESIQEMYAAIKADPDGDGVLSLQEFSNMDLRDFHKYM
RSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRLTRLSPEIVELS
EPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYMT
VLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRV
KPQQGTAVFWYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVD
PSRARQALFQQEMARLAREG
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
6tp5 Chain A Residue 721 [
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Receptor-Ligand Complex Structure
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PDB
6tp5
Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains.
Resolution
2.25 Å
Binding residue
(original residue number in PDB)
D198 N200 D202 H204 Q206 E209
Binding residue
(residue number reindexed from 1)
D87 N89 D91 H93 Q95 E98
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.14.11.29
: hypoxia-inducible factor-proline dioxygenase.
Gene Ontology
Molecular Function
GO:0005506
iron ion binding
GO:0005509
calcium ion binding
GO:0016705
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0031418
L-ascorbic acid binding
View graph for
Molecular Function
External links
PDB
RCSB:6tp5
,
PDBe:6tp5
,
PDBj:6tp5
PDBsum
6tp5
PubMed
33334883
UniProt
Q9NXG6
|P4HTM_HUMAN Transmembrane prolyl 4-hydroxylase (Gene Name=P4HTM)
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