Structure of PDB 1gjw Chain A

Receptor sequence
>1gjwA (length=636) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MLLREINRYCKEKATGKRIYAVPKLWIPGFFKKFDEKSGRCFVDPYELGA
EITDWILNQSREWDYSQPLSFLKGEKTPDWIKRSVVYGSLPRTTAAYNHK
GSGYYEENDVLGFREAGTFFKMMLLLPFVKSLGADAIYLLPVSRMSDLFK
KGDAPSPYSVKNPMELDERYHDPLLEPFKVDEEFKAFVEACHILGIRVIL
DFIPRTAARDSDLIREHPDWFYWIKVEELADYTPPRAEELPFKVPDEDEL
EIIYNKENVKRHLKKFTLPPNLIDPQKWEKIKREEGNILELIVKEFGIIT
PPGFSDLINDPQPTWDDVTFLRLYLDHPEASKRFLDPNQPPYVLYDVIKA
SKFPGKEPNRELWEYLAGVIPHYQKKYGIDGARLDMGHALPKELLDLIIK
NVKEYDPAFVMIAEELDMEKDKASKEAGYDVILGSSWYFAGRVEEIGKLP
DIAEELVLPFLASVETPDTPRIATRKYASKMKKLAPFVTYFLPNSIPYVN
TGQEIGEKQPMNLGLDTDPNLRKVLSPTDEFFGKLAFFDHYVLHWDSPDR
GVLNFIKKLIKVRHEFLDFVLNGKFENLTTKDLVMYSYEKNGQKIVIAAN
VGKEPKEITGGRVWNGKWSDEEKVVLKPLEFALVVQ
3D structure
PDB1gjw The Crystal Structure of Thermotoga Maritima Maltosyltransferase and its Implications for the Molecular Basis of the Novel Transfer Specificity
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 Y158 E414 D468 Y158 E414 D468
BS02 GLC A K151 S156 Y158 D317 K151 S156 Y158 D317
BS03 GLC A G387 H388 L395 E415 A423 S424 A427 Y429 G387 H388 L395 E415 A423 S424 A427 Y429
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0016740 transferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1gjw, PDBe:1gjw, PDBj:1gjw
PDBsum1gjw
PubMed11545590
UniProtO33838

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