Structure of PDB 4f9d Chain A

Receptor sequence
>4f9dA (length=592) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
PWPHNGFVAISWHNVEDEADQRFMSVRTSALREQFAWLRENGYQPVSIAQ
IREAHRGGKPLPEKAVVLTFDDGYQSFYTRVFPILQAFQWPAVWAPVGSW
VDTPADKQVKFGDELVDREYFATWQQVREVARSRLVELASHTWNSHYGIQ
ANATGSLLPVYVNRAYFTDHARYETAAEYRERIRLDAVKMTEYLRTKVEV
NPHVFVWPYGEANGIAIEELKKLGYDMFFTLESGLANASQLDSIPRVLIA
NNPSLKEFAQQIITVQEKSPQRIMHIDLDYVYDENLQQMDRNIDVLIQRV
KDMQISTVYLQAFADPDGDGLVKEVWFPNRLLPMKADIFSRVAWQLRTRS
GVNIYAWMPVLSWDLDPTLTRVKYLPTGEKKAQIHPEQYHRLSPFDDRVR
AQVGMLYEDLAGHAAFDGILFHDDALLSDYEDASAPAITAYQQAGFSGSL
SEIRQNPEQFKQWARFKSRALTDFTLELSARVKAIRGPHIKTARNIFALP
VIQPESEAWFAQNYADFLKSYDWTAIMAMPYLEGVAEKSADQWLIQLTNQ
IKNIPQAKDKSILELQAISSQQLAHWMSLLQLNGVKNYGYYP
3D structure
PDB4f9d The Structure and Metal Dependent Activity of Escherichia coli PgaB Provides Insight into the Partial De-N-acetylation of Poly-b-1,6-N-acetyl-D-glucosamine
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.-
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 CA A D358 D360 D362 L364 D315 D317 D319 L321
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0043708 cell adhesion involved in biofilm formation
GO:0044010 single-species biofilm formation
GO:0098732 macromolecule deacylation
Cellular Component
GO:0009279 cell outer membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4f9d, PDBe:4f9d, PDBj:4f9d
PDBsum4f9d
PubMed22810235
UniProtP75906|PGAB_ECOLI Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase (Gene Name=pgaB)

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