Structure of PDB 4h83 Chain F

Receptor sequence
>4h83F (length=368) Species: 312284 (marine actinobacterium PHSC20C1) [Search protein sequence]
GLTITRIETIPMVAPLAREFRGSHYHMTHRATIVTRVHTDAGIIGEAYTG
DEHETMFDIDRIIHEELAPTLIGQDAMAIERLWDSGYKVTFDILRDRRLG
LVALAAVNTAIWDAVGKALKMPLWKLWGGYRNELPMIAIGGYYGEPLGSI
ADEMHNYQELGLAGVKFKVGGLSAAEDAARITAAREAAGDDFIICIDANQ
GYKPAVAVDLSRRIADLNIRWFEEPVEWHNDKRSMRDVRYQGSVPVCAGQ
TEFSASGCRDLMETGAIDVCNFDSSWSGGPTAWLRTAAIATSYDVQMGHH
EEPQVSTHLLASQPHGTIAECFHPDRDPFWWNMITNRPKLNNGTLTLSDR
PGLGWDLNWDYIDQYRVS
3D structure
PDB4h83 Crystal structure of Mandelate racemase/muconate lactonizing enzyme
ChainF
Resolution2.094 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F38 D69 I157 K184 K186 I214 D215 A216 N217 E241 G267 Q268 N289 D291 H318 E319 E320 E338 D343
Catalytic site (residue number reindexed from 1) F20 D51 I139 K166 K168 I196 D197 A198 N199 E223 G249 Q250 N271 D273 H300 E301 E302 E320 D325
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 BCT F R238 I336 R220 I318
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4h83, PDBe:4h83, PDBj:4h83
PDBsum4h83
PubMed
UniProtA4AFX2

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