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1CHM

ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016980molecular_functioncreatinase activity
B0016787molecular_functionhydrolase activity
B0016980molecular_functioncreatinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CMS A 404
ChainResidue
AHIS232
AHOH563
BPHE62
BARG64
BILE82
ATYR258
AGLU262
APHE320
AHIS324
AARG335
AGLU358
AHOH445
AHOH477

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE CMS B 404
ChainResidue
APHE62
AARG64
AILE82
BALA231
BHIS232
BTYR258
BGLU262
BPHE320
BHIS324
BARG335
BGLU358
BHOH470
BHOH553
BHOH587

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AHIS232
BHIS232

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 1696320
ChainResidueDetails
AHIS232
AGLU262
AGLU358

site_idMCSA1
Number of Residues3
DetailsM-CSA 96
ChainResidueDetails
AHIS232hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU262electrostatic stabiliser, hydrogen bond acceptor
AGLU358electrostatic stabiliser, hydrogen bond acceptor

site_idMCSA2
Number of Residues3
DetailsM-CSA 96
ChainResidueDetails
BHIS232hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLU262electrostatic stabiliser, hydrogen bond acceptor
BGLU358electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2025-06-11

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