Structure of PDB 3f3s Chain A

Receptor sequence
>3f3sA (length=312) Species: 9606 (Homo sapiens) [Search protein sequence]
MAGCVVIVGSGVIGRSWAMLFASGGFQVKLYDIEQQQIRNALENIRKEMK
LLEQAGSLKGSLSVEEQLSLISGCPNIQEAVEGAMHIQECVPEDLELKKK
IFAQLDSIIDDRVILSSSTSCLMPSKLFAGLVHVKQCIVAHPVNPPYYIP
LVELVPHPETAPTTVDRTHALMKKIGQCPMRVQKEVAGFVLNRLQYAIIS
EAWRLVEEGIVSPSDLDLVMSEGLGMRYAFIGPLETMHLNAEGMLSYCDR
YSEGIKHVLQTFGPIPEFSRATAEKVNQDMCMKVPDDPEHLAARRQWRDE
CLMRLAKLKSQV
3D structure
PDB3f3s The Crystal Structure of Human Lambda-Crystallin, CRYL1
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S124 H145 E157 N196
Catalytic site (residue number reindexed from 1) S120 H141 E153 N192
Enzyme Commision number 1.1.1.45: L-gulonate 3-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 NAD A G13 G15 V16 I17 D36 I37 C94 V95 P96 E97 L101 K102 I105 S122 H145 N148 G9 G11 V12 I13 D32 I33 C90 V91 P92 E93 L97 K98 I101 S118 H141 N144
BS02 NAD A N244 Y255 N240 Y251
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042803 protein homodimerization activity
GO:0050104 L-gulonate 3-dehydrogenase activity
GO:0070403 NAD+ binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0019640 D-glucuronate catabolic process to D-xylulose 5-phosphate
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Cellular Component
External links
PDB RCSB:3f3s, PDBe:3f3s, PDBj:3f3s
PDBsum3f3s
PubMed
UniProtQ9Y2S2|CRYL1_HUMAN Lambda-crystallin homolog (Gene Name=CRYL1)

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