Structure of PDB 5m4d Chain A

Receptor sequence
>5m4dA (length=439) Species: 363754 (Rhizobium freirei PRF 81) [Search protein sequence]
GPAMAGNLYGRDGAAIGSLQKLRFFPLAVAGGQGARLVEEDGRELIDLSG
AWGAASLGYGHPAIIEAVSRAAANPAGASILSASNAPAVALAERLTASFP
GRGTHKVWFGHSGSDANEAAYRAITRATGRTGVIAFIGAYHGCTVGSMAF
SGHSVQADAAKADGLILLPYPDPYRPYQDDPTGDAVLALLKERLAAVPAG
SIAAAFIEPIQSDGGLIVPPDGFLRKFADICRAHGISVVCDEVAVGLARS
GRLHCFEHEGFVPDILVLGKGLGGGLPLSAVIAPAEILDCASAFAMQTLH
GNPVCAAAGLAVLETIEAENLTTAAERKGKLLREGLARLAERHELIGDIR
GRGLACGVELVRNRQSREPARAETAKLIYRAYELGLVLYYVGMNGNVLEM
TPPLTMTEDEVRHAVNLLDQAFTELSTVSDTLVSQFAGW
3D structure
PDB5m4d Snapshots of the Catalytic Cycle of the Industrial Enzyme alpha-Amino-epsilon-Caprolactam Racemase (ACLR) Observed Using X-ray Crystallography
ChainA
Resolution1.93 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q17 Y137 E205 D238 A241 K267 T295 E396
Catalytic site (residue number reindexed from 1) Q20 Y140 E208 D241 A244 K270 T298 E399
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 7F7 A W49 S109 G110 S111 Y137 H138 E205 D210 D238 V240 K267 W52 S112 G113 S114 Y140 H141 E208 D213 D241 V243 K270
Gene Ontology
Molecular Function
GO:0008453 alanine-glyoxylate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009436 glyoxylate catabolic process
GO:0019481 L-alanine catabolic process, by transamination

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Molecular Function
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Biological Process
External links
PDB RCSB:5m4d, PDBe:5m4d, PDBj:5m4d
PDBsum5m4d
PubMed
UniProtN6UXY4

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