Structure of PDB 8a0c Chain B

Receptor sequence
>8a0cB (length=1113) Species: 727 (Haemophilus influenzae) [Search protein sequence]
VDKTWLFGSYAWQGNPKALFLYMLVNCKETHECWWVADNEESMKSIKKST
GLKNITFTDSEKAKELFPHADVYVTENFRESYPVYMNENIKVFNTWHGVG
LKHIELALGMNSVLAESIVRKYVRNYDIYKNNVLFLTTSQAMEDHFLEDM
AISKELIIRGKYPRNAVYGPNGIHTYDINTLLPKNKSQYSQTILFCPTYR
IGAIQGVLNSLLPDFAKLEEVCRHKNQLFIVKVHPFMKKDNYFAEMSEKY
KDSEYILFWNDDYDIYEAFNSIDLAIIDYSSIFYDLLDAGVEKFIRYVPD
LDEYQNDLELIGDYADLTEGRIVKSFQQLLNCLDNANIKIISTKRKQYLM
DYFFGFKKENKSMESLIADVDNCQLQPKSLKELHTFDIFDTLIRRSTLRP
FSIFDYVRDKAKASGIKFPLALTENWINVRNRAEHDVRDIMRKTTFERQS
DKIEITLDDIYTRLQKNLLLTDEQTDFLKQAEIEAEIAHVEPIQKRINYL
FSLKAKGHDVAMASDMYLPEDVIYKMLDRADTRLREIPLYLSSTIGYQKS
TGKLYQHIFFDLDYQYSRWTHYGDNKHADGSVPRRLGIQTAVHDIDDFIP
FENAMVNAMDNYNRYPAYQLATKMHRYRTQLVQENGFGNTLFETKYYNYA
YVGASFVPYINWAIKDAIKRGYETIYFISRDGHFLKQIADKIIEIRGYNV
KTKYIYGSRKAWRLPSFITKVDDETFWQFGNFVGMDSFEDLVKASYLSES
ELLSLFPEFESLRHAKHLRGEIAENIRKIFKNSPAYHEKVLAIAAEKRKM
VRQYIQQEINPKEKFAFVEFWGRGYTQDTFGRLLNDAFGKEVKNPFYYVR
SFTDDMGTSVRHNFILAPQNFSFFEPIFAQTPYDSIPDYYEEKGRIEPII
NHRDRSVSDLISEGLLKFTEDYLALNTQDEDYFDAALSQFNYQYQLNTPN
DQFICNVFSELKDNIGVEKPYAPALTLKQLESITSKQELDKLTQSIPISL
SKSDVKVIDYYNKIQKNYNLPAYNSTPMRKAYAVNPLEQYVWSTQVPFRV
LSLKQNSFYLDVSFAETTKRKDIFLKELNEIDVIAVDWLKGGVPRLLTEH
GYITAHKDWVKKS
3D structure
PDB8a0c A multi-enzyme machine polymerizes the Haemophilus influenzae type b capsule.
ChainB
Resolution2.9 Å
3D
structure
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Enzymatic activity
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 PO4 B D386 F388 S513 D514 K548 D387 F389 S514 D515 K549
BS02 PO4 B G821 R822 G823 T825 G822 R823 G824 T826
BS03 PO4 B R679 S884 R680 S885
BS04 C5P B H96 R163 C195 P196 K231 V232 H233 Y265 S279 S280 H97 R164 C196 P197 K232 V233 H234 Y266 S280 S281
BS05 ZN B D386 F388 D573 D387 F389 D574
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0047355 CDP-glycerol glycerophosphotransferase activity
Biological Process
GO:0019350 teichoic acid biosynthetic process
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8a0c, PDBe:8a0c, PDBj:8a0c
PDBsum8a0c
PubMed37277468
UniProtQ2ERG0

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