Structure of PDB 6pxu Chain A Binding Site BS01

Receptor Information

>6pxu Chain A (length=526) Species: 9606 (Homo sapiens)

GPPRTPRPGRREPVMPRPPVPANALGARGEAVRLQLQGEELRLQEESVRL
HQINIYLSDRISLHRRLPERWNPLCKEKKYDYDNLPRTSVIIAFYNEAWS
TLLRTVYSVLETSPDILLEEVILVDDYSDREHLKERLANELSGLPKVRLI
RANKREGLVRARLLGASAARGDVLTFLDCHCECHEGWLEPLLQRIHEEES
AVVCPVIDVIDWNTFEYLGNSGEPQIGGFDWRLVFTWHTVPERERIRMQS
PVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCG
GVLETHPCSHVGHVFPKQAPYSRNKALANSVRAAEVWMDEFKELYYHRNP
RARLEPFGDVTERKQLRDKLQCKDFKWFLETVYPELHVPEDRPGFFGMLQ
NKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNT
HQPEGCIAVEAGMDTLIMHLCEETAPENQKFILQEDGSLFHEQSKKCVQA
ARSFVPLLRDCTNSDHQKWFFKERML

Ligand information

>6pxu Chain C (length=13) Species: 32630 (synthetic construct)

TGYYITPRTGAGA

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6pxu The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its function.
• Resolution: 2.007 Å
• Binding residue (original residue number in PDB): V259 F285 W287 W335 F365 R373
• Binding residue (residue number reindexed from 1): V209 F235 W237 W285 F315 R323

Enzymatic activity

• Enzyme Commision number: 2.4.1.41: polypeptide N-acetylgalactosaminyltransferase.

Gene Ontology

Molecular Function

• GO:0004653 polypeptide N-acetylgalactosaminyltransferase activity
• GO:0005515 protein binding
• GO:0016757 glycosyltransferase activity
• GO:0030246 carbohydrate binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006486 protein glycosylation
• GO:0006493 protein O-linked glycosylation
• GO:0016266 O-glycan processing

Cellular Component

• GO:0000139 Golgi membrane
• GO:0005794 Golgi apparatus
• GO:0016020 membrane

External links

• PDB: RCSB:6pxu, PDBe:6pxu, PDBj:6pxu
• PDBsum: 6pxu
• PubMed: 31548401
• UniProt: Q8IXK2|GLT12_HUMAN Polypeptide N-acetylgalactosaminyltransferase 12 (Gene Name=GALNT12)