Structure of PDB 2v3p Chain A

Receptor sequence
>2v3pA (length=405) Species: 9913 (Bos taurus) [Search protein sequence]
NICEITEVDSTLVERLGQRLLPWMDRLSQEQLNPSIYVGLRLSSLQAGAK
EAHYLHSLKLSYQQSLLRPASNKDDNDSEAKPSMGQLALYLLALRANCEF
IGGRKGDRLVSQLKRFLEDEKRAIGHNHQGHPRTSYYQYSLGILALCVHQ
KRVHDSVVGKLLYAVEHSVDTMAMAGMAFSCLELSNLNPKQRNRINLALK
RVQEKILKAQTPEGYFGNVYSTPLALQLLMGSLRPSVELGTACLKAKAAL
QASLQHKTFQNPLMISQLLPVLNQKSYVDLISPDCQAPRALLEPALETPP
QAKVPKFIDVLLKVSGISPSYRHSVSVPAGSSLEDILKNAQEHGRFRFRT
QASLSGPFLTSVLGRKAGEREFWQVLRDPDTPLQQGIADYRPKDGETIEL
RLVGW
3D structure
PDB2v3p Vitamin B12 Transport Proteins: Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin.
ChainA
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 B12 A G85 Q86 Y137 D179 N227 Y229 S230 M273 Q276 S362 L363 S364 G365 F367 L368 F381 W382 Q383 V384 L392 Q393 G395 W414 G85 Q86 Y137 D170 N218 Y220 S221 M264 Q267 S353 L354 S355 G356 F358 L359 F372 W373 Q374 V375 L383 Q384 G386 W405
Gene Ontology
Molecular Function
GO:0031419 cobalamin binding
GO:0046872 metal ion binding
Biological Process
GO:0006824 cobalt ion transport
GO:0015889 cobalamin transport
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2v3p, PDBe:2v3p, PDBj:2v3p
PDBsum2v3p
PubMed17943552
UniProtQ9XSC9|TCO2_BOVIN Transcobalamin-2 (Gene Name=TCN2)

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