Structure of PDB 1qlt Chain A

Receptor sequence
>1qltA (length=550) Species: 69488 (Penicillium simplicissimum) [Search protein sequence]
EFRPLTLPPKLSLSDFNEFIQDIIRIVGSENVEVISVDGSYMKPTHTHDP
HHVMDQDYFLASAIVAPRNVADVQSIVGLANKFSFPLWPISIGRNSGYGG
AAPRVSGSVVLDMGKNMNRVLEVNVEGAYCVVEPGVTYHDLHNYLEANNL
RDKLWLDVPDLGGGSVLGNAVERGVGYTPYGDHWMMHSGMEVVLANGELL
RTGMGALPDPKRPETMGLKPEDQPWSKIAHLFPYGFGPYIDGLFSQSNMG
IVTKIGIWLMPNPGGYQSYLITLPKDGDLKQAVDIIRPLRLGMALQNVPT
IRHILLDAAVLGDKRSYSSRTEPLSDEELDKIAKQLNLGRWNFYGALYGP
EPIRRVLWETIKDAFSAIPGVKFYFPEDTPENSVLRVRDKTMQGIPTYDE
LKWIDWLPNGAALFFSPIAKVSGEDAMMQYAVTKKRCQEAGLDFIGTFTV
GMREMHHIVCIVFNKKDLIQKRKVQWLMRTLIDDCAANGWGEYRTHLAFM
DQIMETYNWNNSSFLRFNEVLKNAVDPNGIIAPGKSGVWPSQYSHVTWKL
3D structure
PDB1qlt Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y108 D170 E182 D192 D317 V397 E410 I414 A422 H466 Y503 R504 K545
Catalytic site (residue number reindexed from 1) Y98 D160 E172 D182 D307 V387 E400 I404 A412 H456 Y493 R494 K535
Enzyme Commision number 1.1.3.38: vanillyl-alcohol oxidase.
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 FAD A S101 I102 G103 R104 N105 P169 D170 L171 S175 N179 E182 G184 V185 Y187 I261 V262 F424 R504 S91 I92 G93 R94 N95 P159 D160 L161 S165 N169 E172 G174 V175 Y177 I251 V252 F414 R494 MOAD: Kd=4.6mM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004458 D-lactate dehydrogenase (cytochrome) activity
GO:0008720 D-lactate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0018465 vanillyl-alcohol oxidase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0015945 methanol metabolic process
GO:1903457 lactate catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qlt, PDBe:1qlt, PDBj:1qlt
PDBsum1qlt
PubMed10585424
UniProtP56216|VAOX_PENSI Vanillyl-alcohol oxidase (Gene Name=VAOA)

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