Structure of PDB 5c3u Chain A

Receptor sequence
>5c3uA (length=315) Species: 1031333 (Rhizomucor miehei CAU432) [Search protein sequence]
QSLHVATPLLHAPNLTKELECNVFLKMENIQPSGSVKMRGIGAFCYQAVQ
TRGTNIQFVCGSGPNTVLAVSYCARQLGVEAIIVVPKATNERICQSIRTD
GSHLILYGENWTAAEVHARKLVRRNGIYVPSSDHALIWQGHSTIVQELKT
QLNDNPPAAIICPVGGGGLLNGVIMGLQEADWKDVPVIAVETHGSNAFQA
SVVAGELVIMEKNNTIATSLISKAVSSKSLELSLNHPVVPFAVSDAMAAD
AVRLFAEDFKMLVEASAGAALSLCYTHLIRDILPSLSPAKDVVVLVTGGS
DISLAHLDEYRKKYM
3D structure
PDB5c3u Crystal structure and characterization of a novel l-serine ammonia-lyase from Rhizomucor miehei.
ChainA
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K52 G78 E206 S210 A212 S234 T312
Catalytic site (residue number reindexed from 1) K37 G63 E191 S195 A197 S219 T297
Enzyme Commision number 4.3.1.17: L-serine ammonia-lyase.
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 A K52 N80 S147 P178 G180 G181 G182 G183 S234 T312 K37 N65 S132 P163 G165 G166 G167 G168 S219 T297
Gene Ontology
Molecular Function
GO:0003941 L-serine ammonia-lyase activity
GO:0004794 threonine deaminase activity
Biological Process
GO:0006565 L-serine catabolic process
GO:0006567 threonine catabolic process
GO:0009097 isoleucine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5c3u, PDBe:5c3u, PDBj:5c3u
PDBsum5c3u
PubMed26367174
UniProtA0A0X1KHE6

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