Structure of PDB 6qkb Chain B

Receptor sequence
>6qkbB (length=383) Species: 266 (Paracoccus denitrificans) [Search protein sequence]
TDFSGYEVGYDIPALPGMDESEIQTPCLILDLDALERNIRKMGDYAKAHG
MRHRSHGKMHKSVDVQKLQESLGGSVGVCCQKVSEAEAFARGGIKDVLVT
NEVREPAKIDRLARLPKTGATVTVCVDDVQNIADLSAAAQKHGTELGIFV
EIDCGAGRCGVTTKEAVVEIAKAAAAAPNLTFKGIQAYQGAMQHMDSFED
RKAKLDAAIAQVKEAVDALEAEGLAPEFVSGGGTGSYYFESNSGIYNELQ
CGSYAFMDADYGRIHDAEGKRIDQGEWENALFILTSVMSHAKPHLAVVDA
GLKAQSVDSGLPFVYGRDDVKYIKCSDEHGVVEDKDGVLKVNDKLRLVPG
HCDPTCNVHDWYVGVRNGKVETVWPVSARGKGY
3D structure
PDB6qkb Marine Proteobacteria metabolize glycolate via the beta-hydroxyaspartate cycle.
ChainB
Resolution1.701 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.3.41: 3-hydroxy-D-aspartate aldolase.
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 PLP B H60 K62 Q85 Y192 T238 Q254 G256 S257 Y265 H56 K58 Q81 Y188 T234 Q250 G252 S253 Y261
BS02 MG B H355 D357 H351 D353
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008721 D-serine ammonia-lyase activity
GO:0016829 lyase activity
GO:0016833 oxo-acid-lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0046872 metal ion binding
Biological Process
GO:0009436 glyoxylate catabolic process
GO:0036088 D-serine catabolic process
GO:0046296 glycolate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6qkb, PDBe:6qkb, PDBj:6qkb
PDBsum6qkb
PubMed31723261
UniProtA1B8Z1|BHCC_PARDP 3-hydroxy-D-aspartate aldolase (Gene Name=bhcC)

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