Structure of PDB 1hfz Chain C

Receptor sequence
>1hfzC (length=122) Species: 9913 (Bos taurus) [Search protein sequence]
MEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTE
YGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIVCVKKILDKV
GINYWLAHKALCSEKLDQWLCE
3D structure
PDB1hfz Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase.
ChainC
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T33 N45 S47 E49 N56
Catalytic site (residue number reindexed from 1) T34 N46 S48 E50 N57
Enzyme Commision number 2.4.1.22: lactose synthase.
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 CA C K79 D82 D84 D87 D88 K80 D83 D85 D88 D89
Gene Ontology
Molecular Function
GO:0003796 lysozyme activity
GO:0004461 lactose synthase activity
GO:0005509 calcium ion binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0005989 lactose biosynthetic process
GO:0032355 response to estradiol
GO:0032570 response to progesterone
GO:1903494 response to dehydroepiandrosterone
GO:1903496 response to 11-deoxycorticosterone
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1hfz, PDBe:1hfz, PDBj:1hfz
PDBsum1hfz
PubMed8805552
UniProtP00711|LALBA_BOVIN Alpha-lactalbumin (Gene Name=LALBA)

[Back to BioLiP]