Structure of PDB 6gqd Chain A

Receptor sequence
>6gqdA (length=344) Species: 9606 (Homo sapiens) [Search protein sequence]
YTPFLANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQLLKTVPRHDPLNPL
CPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAKSARG
VCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENK
GAMMGCSNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQ
ELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDD
LASIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGANWDHWQLHAHYYP
PLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHYHL
3D structure
PDB6gqd Structure of human galactose-1-phosphate uridylyltransferase (GALT), with crystallization epitope mutations A21Y:A22T:T23P:R25L
ChainA
Resolution1.523 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N72 C75 S135 N173 S181 H184 H186 Q188
Catalytic site (residue number reindexed from 1) N48 C51 S111 N149 S157 H160 H162 Q164
Enzyme Commision number 2.7.7.12: UDP-glucose--hexose-1-phosphate uridylyltransferase.
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 ZN A E202 H301 H319 H321 E178 H277 H295 H297
BS02 H2U A P73 A81 N97 D98 H186 Q188 P49 A57 N73 D74 H162 Q164
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008108 UDP-glucose:hexose-1-phosphate uridylyltransferase activity
GO:0008270 zinc ion binding
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006011 UDP-glucose metabolic process
GO:0006012 galactose metabolic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005737 cytoplasm
GO:0005794 Golgi apparatus
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6gqd, PDBe:6gqd, PDBj:6gqd
PDBsum6gqd
PubMed
UniProtP07902|GALT_HUMAN Galactose-1-phosphate uridylyltransferase (Gene Name=GALT)

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