Structure of PDB 2puv Chain D

Receptor sequence
>2puvD (length=340) Species: 237561 (Candida albicans SC5314) [Search protein sequence]
PYKHFMQKEIFEQPDSAFNTMRGRIDFENCVVTLGGLKSWLSTIRRCRRI
IMIACGTSYHSCLATRSIFEELTEIPVSVELASDFLDRRSPVFRDDTCVF
VSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPE
IGVASTKAYTSQYIALVMFALSLSNDSISRKGRHEEIIKGLQKIPEQIKQ
VLKLENKIKDLCNSSLNDQKSLLLLGRGYQFATALEGALKIKEISYMHSE
GVLAGELLPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDAIISN
DKVHTTLEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDV
3D structure
PDB2puv The Crystal and Solution Studies of Glucosamine-6-phosphate Synthase from Candida albicans
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E584 K588 E591
Catalytic site (residue number reindexed from 1) E236 K240 E243
Enzyme Commision number 2.6.1.16: glutamine--fructose-6-phosphate transaminase (isomerizing).
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 UD1 D R372 G384 G474 V476 S484 T487 C489 G490 V491 H492 R24 G36 G126 V128 S136 T139 C141 G142 V143 H144
BS02 M6R D C403 T405 S406 S450 Q451 S452 T455 A502 S503 E591 C55 T57 S58 S102 Q103 S104 T107 A154 S155 E243
Gene Ontology
Molecular Function
GO:0097367 carbohydrate derivative binding
Biological Process
GO:1901135 carbohydrate derivative metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2puv, PDBe:2puv, PDBj:2puv
PDBsum2puv
PubMed17681543
UniProtP53704|GFA1_CANAL Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (Gene Name=GFA1)

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