Structure of PDB 6tp5 Chain A

Receptor sequence
>6tp5A (length=370) Species: 9606 (Homo sapiens) [Search protein sequence]
TLGPLTRLEGIKVGHERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEEC
RLIIHLAQMKGLQRSQILPTEEYEEQVSQLDLFRLLDQNRDGHLQLREVL
AQTRLGNGWWMTPESIQEMYAAIKADPDGDGVLSLQEFSNMDLRDFHKYM
RSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRLTRLSPEIVELS
EPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYMT
VLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRV
KPQQGTAVFWYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVD
PSRARQALFQQEMARLAREG
3D structure
PDB6tp5 Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains.
ChainA
Resolution2.25 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.29: hypoxia-inducible factor-proline dioxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 OGA A Y319 H328 T375 H441 K451 N455 Y208 H217 T264 H330 K340 N344
BS02 FE2 A H328 D330 H441 H217 D219 H330
BS03 CA A D198 N200 D202 H204 Q206 E209 D87 N89 D91 H93 Q95 E98
BS04 CA A D237 D239 D241 V243 E248 D126 D128 D130 V132 E137
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
PDBsum6tp5
PubMed33334883
UniProtQ9NXG6|P4HTM_HUMAN Transmembrane prolyl 4-hydroxylase (Gene Name=P4HTM)

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