Structure of PDB 1h5q Chain D

Receptor sequence
>1h5qD (length=260) Species: 5341 (Agaricus bisporus) [Search protein sequence]
PGFTISFVNKTIIVTGGNRGIGLAFTRAVAAAGANVAVIYRSAADAVEVT
EKVGKEFGVKTKAYQCDVSNTDIVTKTIQQIDADLGPISGLIANAGVSVV
KPATELTHEDFAFVYDVNVFGVFNTCRAVAKLWLQKQQKGSIVVTSSMSS
QIINQSSLNGSLTQVFYNSSKAACSNLVKGLAAEWASAGIRVNALSPGYV
NTDQTAHMDKKIRDHQASNIPLNRFAQPEEMTGQAILLLSDHATYMTGGE
YFIDGGQLIW
3D structure
PDB1h5q The Crystallographic Structure of the Mannitol 2-Dehydrogenase Nadp+ Binary Complex from Agaricus Bisporus
ChainD
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G22 S149 Y169 K173
Catalytic site (residue number reindexed from 1) G20 S147 Y167 K171
Enzyme Commision number 1.1.1.138: mannitol 2-dehydrogenase (NADP(+)).
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 NAP D G18 N20 R21 G22 I23 Y42 R43 S44 A45 C68 D69 V70 N96 A97 G98 V99 T147 S149 Y169 K173 P199 G200 V202 Q206 G16 N18 R19 G20 I21 Y40 R41 S42 A43 C66 D67 V68 N94 A95 G96 V97 T145 S147 Y167 K171 P197 G198 V200 Q204
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0050085 mannitol 2-dehydrogenase (NADP+) activity
GO:0050661 NADP binding
GO:0050664 oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
Biological Process
GO:0019594 mannitol metabolic process
GO:0051289 protein homotetramerization

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Molecular Function
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Biological Process
External links
PDB RCSB:1h5q, PDBe:1h5q, PDBj:1h5q
PDBsum1h5q
PubMed11335726
UniProtO93868|NMTDH_AGABI NADP-dependent mannitol dehydrogenase (Gene Name=mtdH)

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