Structure of PDB 6j3x Chain A

Receptor sequence
>6j3xA (length=415) Species: 304 (Roseateles saccharophilus) [Search protein sequence]
DQAGKSPAGVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQASTIAADG
FSAIWMPVPWRDFSSWTKSGGGEGYFWHDFNKNGRYGSDAQLRQAAGALG
GAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDCDDG
DRFIGGESDLNTGHPQIYGMFRDELANLRSGYGAGGFRFDFVRGYAPERV
NSWMTDSADSSFCVGELWKGPSEYPSWDWRNTASWQQIIKDWSDRAKCPV
FDFALKERMQNGSVADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPGQNG
GQHHWALQDGLIRQAYAYILTSPGTPVVYWSHMYDWGYGDFIRQLIQVRR
TAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLANPGQVASGSFS
EAVNASNGQVRVWRS
3D structure
PDB6j3x Maltotetraose-forming amylase from Pseudomonas saccharophila STB07
ChainA
Resolution1.62 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R191 D193 E219 H293 D294
Catalytic site (residue number reindexed from 1) R188 D190 E216 H290 D291
Enzyme Commision number 3.2.1.60: glucan 1,4-alpha-maltotetraohydrolase.
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 GLC A W25 F156 Q305 W25 F153 Q302
BS02 GLC A W66 F79 W66 F76
BS03 GLC A I157 G158 E160 I154 G155 E157
BS04 CA A D1 Q2 H13 D16 E17 D1 Q2 H13 D16 E17
BS05 CA A N116 D151 D154 D162 G197 N113 D148 D151 D159 G194
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
GO:0033910 glucan 1,4-alpha-maltotetraohydrolase activity
GO:0043169 cation binding
GO:0046872 metal ion binding
GO:2001070 starch binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005983 starch catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6j3x, PDBe:6j3x, PDBj:6j3x
PDBsum6j3x
PubMed
UniProtP22963|AMT4_ROSSA Glucan 1,4-alpha-maltotetraohydrolase (Gene Name=mta)

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