Structure of PDB 4atf Chain D

Receptor sequence
>4atfD (length=297) Species: 63186 (Zobellia galactanivorans) [Search protein sequence]
VDWKDIPVPADAGPNMKWEFQEISDNFEYEAPADNKGSEFLEKWDDFYHN
AWAGPGLTEWKRDRSYVADGELKMWATRKPGSDKINMGCITSKTRVVYPV
YIEARAKVMNSTLASDVWLLSADDTQEIDILDAYGADYSESAGKDHSYFS
KKVHISHHVFIRDPFQDYQPKDAGSWFEDGTVWNKEFHRFGVYWRDPWHL
EYYIDGVLVRTVSGKDIIDPKHFTNTTDPGNTEIDTRTGLNKEMDIIINT
EDQTWRSSPASGLQSNTYTPTDNELSNIENNTFGVDWIRIYKPVEKL
3D structure
PDB4atf Biochemical and Structural Characterization of the Complex Agarolytic Enzyme System from the Marine Bacterium Zobellia Galactanivorans.
ChainD
Resolution1.9 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D Y205 F206 Y148 F149
BS02 AAL D F206 W233 W312 F149 W176 W255
BS03 GAL D H211 Q226 W312 H154 Q169 W255
BS04 AAL D D186 D189 H211 H215 Q226 Q310 D129 D132 H154 H158 Q169 Q253
BS05 GAL D D173 W175 H215 E308 D116 W118 H158 E251
BS06 AAL D Y105 W175 R219 Y48 W118 R162
BS07 GAL D 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4atf, PDBe:4atf, PDBj:4atf
PDBsum4atf
PubMed22778272
UniProtQ9RGX8|AGAB_ZOBGA Beta-agarase B (Gene Name=agaB)

[Back to BioLiP]