Structure of PDB 4atf Chain B

Receptor sequence
>4atfB (length=296) Species: 63186 (Zobellia galactanivorans) [Search protein sequence]
VDWKDIPVPADAGPNMKWEFQEISDNFEYEAPADNKGSEFLEKWDDFYHN
AWAGPGLTEWKRDRSYVADGELKMWATRKPGSDKINMGCITSKTRVVYPV
YIEARAKVMNSTLASDVWLLSADDTQEIDILDAYGADYSESAGKDHSYFS
KKVHISHHVFIRDPFQDYQPKDAGSWFEDGTVWNKEFHRFGVYWRDPWHL
EYYIDGVLVRTVSGKDIIDPKHFTNTTDPGNTEIDTRTGLNKEMDIIINT
EDQTWRSSPASGLQSNTYTPTDNELSNIENNTFGVDWIRIYKPVEK
3D structure
PDB4atf Biochemical and Structural Characterization of the Complex Agarolytic Enzyme System from the Marine Bacterium Zobellia Galactanivorans.
ChainB
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.81: beta-agarase.
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 GAL B Y205 F206 Y148 F149
BS02 GAL B H211 Q226 W312 H154 Q169 W255
BS03 AAL B D189 Y191 H211 H215 Q310 D132 Y134 H154 H158 Q253
BS04 GAL B D173 W175 E184 H215 E308 D116 W118 E127 H158 E251
BS05 AAL B Y105 R219 Y48 R162
BS06 GAL B Y105 W109 D181 R219 Y48 W52 D124 R162
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033916 beta-agarase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0005975 carbohydrate metabolic process
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:4atf, PDBe:4atf, PDBj:4atf
PDBsum4atf
PubMed22778272
UniProtQ9RGX8|AGAB_ZOBGA Beta-agarase B (Gene Name=agaB)

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