Structure of PDB 1chm Chain B

Receptor sequence
>1chmB (length=401) Species: 303 (Pseudomonas putida) [Search protein sequence]
QMPKTLRIRNGDKVRSTFSAQEYANRQARLRAHLAAENIDAAIFTSYHNI
NYYSDFLYCSFGRPYALVVTEDDVISISANIDGGQPWRRTVGTDNIVYTD
WQRDNYFAAIQQALPKARRIGIEHDHLNLQNRDKLAARYPDAELVDVAAA
CMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQA
MVRAIADTFEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKGDILSLNCF
PMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDI
ARELNEIFLKHDVLQYRTFGYGHSFGTLSHYYGREAGLELREDIDTVLEP
GMVVSMEPMIMLPEGLPGAGGYREHDILIVNENGAENITKFPYGPEKNII
R
3D structure
PDB1chm Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H232 E262 E358
Catalytic site (residue number reindexed from 1) H231 E261 E357
Enzyme Commision number 3.5.3.3: creatinase.
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 CMS B F62 R64 I82 F61 R63 I81 MOAD: Ki=0.22mM
BS02 CMS B H232 E262 F320 H324 R335 E358 H231 E261 F319 H323 R334 E357 MOAD: Ki=0.22mM
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016980 creatinase activity

View graph for
Molecular Function
External links
PDB RCSB:1chm, PDBe:1chm, PDBj:1chm
PDBsum1chm
PubMed1696320
UniProtP38488|CREA_PSEPU Creatinase

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