Structure of PDB 2clp Chain J

Receptor sequence
>2clpJ (length=323) Species: 9606 (Homo sapiens) [Search protein sequence]
RPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETIL
GGLGLRLGGSDCRVKIDTKAIPLFGNSLKPDSLRFQLETSLKRLQCPRVD
LFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCK
SNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGK
YKYEDKDGKQPVGRFFGNTWAEMYRNRYWKEHHFEGIALVEKALQAAYGA
SAPSMTSATLRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAAAEEGPLE
PAVVDAFNQAWHLVAHECPNYFR
3D structure
PDB2clp Crystal Structure of Human Aflatoxin B1 Aldehyde Reductase Member 3
ChainJ
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D73 Y78 P109 H142
Catalytic site (residue number reindexed from 1) D36 Y41 P72 H105
Enzyme Commision number 1.-.-.-
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 NDP J G44 M46 D73 Y78 H142 Q198 F226 N227 P228 L229 G231 G232 T235 K237 G250 R251 I315 G317 M318 S319 Q323 N327 G7 M9 D36 Y41 H105 Q161 F189 N190 P191 L192 G194 G195 T198 K200 G213 R214 I278 G280 M281 S282 Q286 N290
Gene Ontology
Molecular Function
GO:0004033 aldo-keto reductase (NADPH) activity
GO:0005515 protein binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006081 cellular aldehyde metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2clp, PDBe:2clp, PDBj:2clp
PDBsum2clp
PubMed
UniProtO95154|ARK73_HUMAN Aflatoxin B1 aldehyde reductase member 3 (Gene Name=AKR7A3)

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