Structure of PDB 3uva Chain C

Receptor sequence
>3uvaC (length=405) Species: 86665 (Halalkalibacterium halodurans) [Search protein sequence]
SMKSQFERAKIEYGQWGIDVEEALERLKQVPISIHCFQGDDVGGFELSGD
YPGKATTPEELRMDLEKALSLIPGKHRVNLHAIYAETDGKVVERDQLEPR
HFEKWVRWAKRHGLGLDFNPTLFSHEKAKDGLTLAHPDQAIRQFWIDHCI
ASRKIGEYFGKELETPCLTNIWIPDGYKDTPSDRLTPRKRLKESLDQIFA
AEINEAYNLDAVESKLFGIGSESYVVGSHEFYLSYALKNDKLCLLDTGHY
HPTETVSNKISAMLLFHDKLALHVSRPVRWDSDHVVTFDDELREIALEIV
RNDALDRVLIGLDFFDASINRIAAWTIGTRNVIKALLFAMLIPHKQLKEW
QETGDYTRRLAVLEEFKTYPLGAIWNEYCERMNVPIKEEWLKEIAIYEKE
VLLQR
3D structure
PDB3uva Structure-based studies on the metal binding of two-metal-dependent sugar isomerases.
ChainC
Resolution2.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W184 E225 K227 D258 H261 H285 D293 D295 D325
Catalytic site (residue number reindexed from 1) W172 E213 K215 D246 H249 H273 D281 D283 D313
Enzyme Commision number 5.3.1.14: L-rhamnose isomerase.
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 MN C E225 D258 H261 H285 D325 E213 D246 H249 H273 D313
BS02 MN C D258 H261 D293 D295 D246 H249 D281 D283
Gene Ontology
Molecular Function
GO:0008740 L-rhamnose isomerase activity
GO:0016853 isomerase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0019299 rhamnose metabolic process
GO:0019301 rhamnose catabolic process
GO:0019324 L-lyxose metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3uva, PDBe:3uva, PDBj:3uva
PDBsum3uva
PubMed24925069
UniProtQ9KCL9|RHAA_HALH5 L-rhamnose isomerase (Gene Name=rhaA)

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