Structure of PDB 5hj5 Chain B

Receptor sequence
>5hj5B (length=267) Species: 243277 (Vibrio cholerae O1 biovar El Tor str. N16961) [Search protein sequence]
MRLIPLKAAAQVGKWAAAHIVKRINEFQPTAERPFVLGLPTGGTPLATYK
ALIEMHKAGEVSFKHVVTFNMDEYVGLAADHPESYRSFMYNNFFNHIDIQ
EENINLLNGNTDDHEAECKRYEDKIKSYGKINLFMGGVGNDGHIAFNEPA
SSLSSRTRIKTLTEDTRIANSRFFDGDINQVPKYALTIGVGTLLDAQEIM
ILVTGHNKALALQAAVEGSVNHLWTVSALQLHPKAVIVCDEPSTQELKVK
TVKYFTELEAKNIVGFR
3D structure
PDB5hj5 Crystal structure of tertiary complex of glucosamine-6-phosphate deaminase from Vibrio cholerae with BETA-D-GLUCOSE-6-PHOSPHATE and FRUCTOSE -6-PHOSPHATE
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D72 D141 H143 E148
Catalytic site (residue number reindexed from 1) D72 D141 H143 E148
Enzyme Commision number 3.5.99.6: glucosamine-6-phosphate deaminase.
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 F6R B T41 G42 G43 T44 D72 G137 V138 H143 A145 R172 K208 T41 G42 G43 T44 D72 G137 V138 H143 A145 R172 K208
BS02 BG6 B M1 R2 M1 R2
Gene Ontology
Molecular Function
GO:0004342 glucosamine-6-phosphate deaminase activity
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006043 glucosamine catabolic process
GO:0006044 N-acetylglucosamine metabolic process
GO:0006046 N-acetylglucosamine catabolic process
GO:0019262 N-acetylneuraminate catabolic process
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:5hj5, PDBe:5hj5, PDBj:5hj5
PDBsum5hj5
PubMed
UniProtQ9KKS5|NAGB_VIBCH Glucosamine-6-phosphate deaminase (Gene Name=nagB)

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