Structure of PDB 2iy4 Chain V

Receptor sequence
>2iy4V (length=150) Species: 1639 (Listeria monocytogenes) [Search protein sequence]
VDTKEFLNHQVANLNVFTVKIHQIHWYMRGHNFFTLHEKMDDLYSEFGEQ
MDEVAERLLAIGGSPFSTLKEFLENASVEEAPYTKPKTMDQLMEDLVGTL
ELLRDEYQQGIELTDKEGDNVTNDMLIAFKASIDKHIWMFKAFLGKAPLE
3D structure
PDB2iy4 The Mutations Lys 114 --> Gln and Asp 126 --> Asn Disrupt an Intersubunit Salt Bridge and Convert Listeria Innocua Dps Into its Natural Mutant Listeria Monocytogenes Dps. Effects on Protein Stability at Low Ph.
ChainV
Resolution2.31 Å
3D
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
Enzyme Commision number 1.16.-.-
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 FE V D58 E62 D52 E56
BS02 FE V H31 D47 H25 D41
Gene Ontology
Molecular Function
GO:0008199 ferric iron binding
GO:0016491 oxidoreductase activity
GO:0016722 oxidoreductase activity, acting on metal ions
GO:0046872 metal ion binding
Biological Process
GO:0006879 intracellular iron ion homeostasis
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2iy4, PDBe:2iy4, PDBj:2iy4
PDBsum2iy4
PubMed17186524
UniProtQ8Y8G1|DPS_LISMO DNA protection during starvation protein (Gene Name=dps)

[Back to BioLiP]