Structure of PDB 2x1i Chain A

Receptor sequence
>2x1iA (length=497) Species: 56956 (Thermus brockianus) [Search protein sequence]
PCAYGLLLHPTSLPGPWGVGVLGEEARGFLRFLKEAGARYWQVLPLGPTG
YGDSPYQSFSAFAGNPYLIDLRPLVDRGFVRLEDPGFPEGRVDYGLLYAW
KWPALRAAFQGFRQKASPEEKEDFARFQEEEAWWLRDYALFMTLKSHHGG
LPWNAWPLALRTREERALKEAEASLAEEIAFHAFTQWLFFRQWGALKEEA
EALGIAFIGDMPIFVAEDSAEVWAHPEWFHLDEEGRPTVVAGVPPDYFSE
TGQRWGNPLYRWEVLEEEGFSFWIARLRKALELFHLVRIDHFRGFEAYWE
IPASCPTAVEGRWVKAPGEKLFARIQEAFGRIPILAEDLGVITPEVEALR
DRFGLPGMKVLQFAFDNGMENPFLPHNYPEHGRVVVYTGTHDNDTTLGWY
RTATPHERDFLKRYLADWGITFREEAEVPWALMRLGMASRARLAVYPVQD
VLALGSEARMNYPGRPSGNWAWRLRPGEIKEEHGERLLSLAEATGRV
3D structure
PDB2x1i Structural and Functional Analysis of Substrate Recognition by the 250S Loop in Amylomaltase from Thermus Brockianus.
ChainA
Resolution2.36 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D293 E340 D395
Catalytic site (residue number reindexed from 1) D290 E337 D392
Enzyme Commision number 2.4.1.25: 4-alpha-glucanotransferase.
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 INS A C5 R42 C2 R39
BS02 INS A E27 R30 R34 E24 R27 R31
Gene Ontology
Molecular Function
GO:0004134 4-alpha-glucanotransferase activity
GO:0016757 glycosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2x1i, PDBe:2x1i, PDBj:2x1i
PDBsum2x1i
PubMed21117235
UniProtQ2VJA0

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