Structure of PDB 6k5z Chain B

Receptor sequence
>6k5zB (length=314) Species: 178306 (Pyrobaculum aerophilum str. IM2) [Search protein sequence]
MEIRKDPFTGEYILVSPHRLKRPWQPEGACPFCPGAPETGRGWDVLILPN
RYPVVTENPPEPTAEDLYEVIPARGSSLVVVETPQHDVDDLSDLPLGQIK
KILTAVAEAQRKAEKEGNAAYFLFFRNKGKEIGVSLTHPHSQIYILPVVP
PRVRAELQASYEWYVKHGSCLHCRIVEKEEKRLVFQNRNWKAFVPFYAKW
PHEVHIYPKRHRSLLTELTDEEVADLAEALKITLCALKQVAGIPMPYIMV
LHQAPLPRPTQYYHLHFEIYGMYRPDGKLKHAAGAELGASLFTLDTTPEE
TAARIKAALQKCLK
3D structure
PDB6k5z Unique active site formation in a novel galactose 1-phosphate uridylyltransferase from the hyperthermophilic archaeon Pyrobaculum aerophilum.
ChainB
Resolution2.33 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C30 C33 H86 N127 S135 H138 H140 Q142
Catalytic site (residue number reindexed from 1) C30 C33 H86 N127 S135 H138 H140 Q142
Enzyme Commision number ?
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 B C30 C33 H86 H138 C30 C33 H86 H138
BS02 ZN B C170 C173 H211 H264 C170 C173 H211 H264
BS03 FE B E156 H252 H266 E268 E156 H252 H266 E268
BS04 PO4 B V134 S135 L136 H140 V134 S135 L136 H140
Gene Ontology
Molecular Function
GO:0000166 nucleotide 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:0005975 carbohydrate metabolic process
GO:0006012 galactose metabolic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6k5z, PDBe:6k5z, PDBj:6k5z
PDBsum6k5z
PubMed31693208
UniProtQ8ZXN7

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