Structure of PDB 1t2a Chain C

Receptor sequence

>1t2aC (length=338) Species: 9606 (Homo sapiens)

RNVALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTGRIEHLYNMK
LHYGDLTDSTCLVKIINEVKPTEIYNLGAQSHVKISFDLAEYTADVDGVG
TLRLLDAVKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGA
AKLYAYWIVVNFREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIY
LGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATGEVHSV
REFVEKSFLHIGKTIVWEGKNENEVGRCKETGKVHVTVDLKYYRPTEVDF
LQGDCTKAKQKLNWKPRVAFDELVREMVHADVELMRTN

3D structure

• PDB: 1t2a Crystal Structure and Biophysical Characterization of Human GDP-D-mannose 4,6-dehydratase
• Chain: C
• Resolution: 1.84 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T155 S156 E157 Y179 K183
• Catalytic site (residue number reindexed from 1): T124 S125 E126 Y148 K152
• Enzyme Commision number: 4.2.1.47: GDP-mannose 4,6-dehydratase.

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	C	R56 S58	R34 S36
BS02	NDP	C	G30 T32 G33 Q34 D35 R55 D86 L87 L108 G109 A110 S112 A153 S154 T155 Y179 K183 L206 N208 H209 R214	G8 T10 G11 Q12 D13 R33 D55 L56 L77 G78 A79 S81 A122 S123 T124 Y148 K152 L175 N177 H178 R183
BS03	GDP	C	N208 V219 K222 G241 N242 R247 R325 E328	N177 V188 K191 G210 N211 R216 R294 E297

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• GO:0008446 GDP-mannose 4,6-dehydratase activity
• GO:0016829 lyase activity
• GO:0042802 identical protein binding
• GO:0070401 NADP+ binding

Biological Process

• GO:0007219 Notch signaling pathway
• GO:0019673 GDP-mannose metabolic process
• GO:0042350 GDP-L-fucose biosynthetic process
• GO:0042351 'de novo' GDP-L-fucose biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:1t2a, PDBe:1t2a, PDBj:1t2a
• PDBsum: 1t2a
• UniProt: O60547|GMDS_HUMAN GDP-mannose 4,6 dehydratase (Gene Name=GMDS)