Structure of PDB 1p4c Chain A

Receptor sequence
>1p4cA (length=353) Species: 303,3562 [Search protein sequence]
NLFNVEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKR
LVDVSRRSLQAEVLGKRQSMPLLIGPTGLNGALWPKGDLALARAATKAGI
PFVLSTASNMSIEDLARQCDGDLWFQLYVIHREIAQGMVLKALHTGYTTL
VLTTDVAVNGYRERDLHNRFKIPPFLTLKNFEGIDLGKMDKANLEMQAAL
MSRQMDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRCIAEGADGVILS
NHGGRQLDCAISPMEVLAQSVAKTGKPVLIDSGFRRGSDIVKALALGAEA
VLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSPDYL
QNE
3D structure
PDB1p4c High Resolution Structures of an Oxidized and Reduced Flavoprotein: THE WATER SWITCH IN A SOLUBLE FORM OF (S)-MANDELATE DEHYDROGENASE
ChainA
Resolution1.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S108 Y131 T156 D158 K231 H255
Catalytic site (residue number reindexed from 1) S105 Y128 T153 D155 K228 H252
Enzyme Commision number 1.1.3.15: (S)-2-hydroxy-acid oxidase.
1.1.99.31: (S)-mandelate dehydrogenase.
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 FMN A Y26 P79 T80 G81 S108 Q129 Y131 T156 K231 H255 G256 R258 D284 S285 G286 R288 G307 R308 Y23 P76 T77 G78 S105 Q126 Y128 T153 K228 H252 G253 R255 D281 S282 G283 R285 G304 R305
Gene Ontology
Molecular Function
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:1p4c, PDBe:1p4c, PDBj:1p4c
PDBsum1p4c
PubMed14604988
UniProtP05414|GOX_SPIOL Glycolate oxidase;
P20932|MDLB_PSEPU (S)-mandelate dehydrogenase (Gene Name=mdlB)

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