Structure of PDB 1nba Chain C

Receptor sequence
>1nbaC (length=253) Species: 1667 (Arthrobacter sp.) [Search protein sequence]
TFNDIEARLAAVLEEAFEAGTSIYNERGFKRRIGYGNRPAVIHIDLANAW
TQPGHPFSCPGMETIIPNVQRINEAARAKGVPVFYTTNVYRNRDASSGTN
DMGLWYSKIPTETLPADSYWAQIDDRIAPADGEVVIEKNRASAFPGTNLE
LFLTSNRIDTLIVTGATAAGCVRHTVEDAIAKGFRPIIPRETIGDRVPGV
VQWNLYDIDNKFGDVESTDSVVQYLDALPQFEDTVPKTLSDPQPEVEAPA
DPV
3D structure
PDB1nba Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution.
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D51 K144 A172 T173 C177
Catalytic site (residue number reindexed from 1) D45 K138 A166 T167 C171
Enzyme Commision number 3.5.1.59: N-carbamoylsarcosine amidase.
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 SO4 C W56 T173 C177 R202 W50 T167 C171 R196
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0050127 N-carbamoylsarcosine amidase activity
Biological Process
GO:0006602 creatinine catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1nba, PDBe:1nba, PDBj:1nba
PDBsum1nba
PubMed1381445
UniProtP32400|CSH_ARTSP N-carbamoylsarcosine amidase

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