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2Y7F

Crystal structure of the 3-keto-5-aminohexanoate cleavage enzyme (Kce) from C. Cloacamonas acidaminovorans in complex with the substrate 3- keto-5-aminohexanoate

Functional Information from GO Data
ChainGOidnamespacecontents
A0016740molecular_functiontransferase activity
A0019475biological_processL-lysine catabolic process to acetate
A0043720molecular_function3-keto-5-aminohexanoate cleavage activity
A0046872molecular_functionmetal ion binding
B0016740molecular_functiontransferase activity
B0019475biological_processL-lysine catabolic process to acetate
B0043720molecular_function3-keto-5-aminohexanoate cleavage activity
B0046872molecular_functionmetal ion binding
C0016740molecular_functiontransferase activity
C0019475biological_processL-lysine catabolic process to acetate
C0043720molecular_function3-keto-5-aminohexanoate cleavage activity
C0046872molecular_functionmetal ion binding
D0016740molecular_functiontransferase activity
D0019475biological_processL-lysine catabolic process to acetate
D0043720molecular_function3-keto-5-aminohexanoate cleavage activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS46
AHIS48
AGLU230
AKMH1276
AHOH2236

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE KMH A 1276
ChainResidue
AGLY84
AGLY85
AVAL87
ATHR106
AASN108
APHE114
ATYR145
AGLU230
AZN301
AHOH2007
AHOH2236
AHOH2237
AGLU14
AHIS46
AHIS48
ASER82

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS46
BHIS48
BGLU230
BKMH1276
BHOH2228

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE KMH B 1276
ChainResidue
BGLU14
BHIS46
BHIS48
BSER82
BGLY84
BGLY85
BVAL87
BTHR106
BASN108
BPHE114
BTYR145
BGLU230
BZN301
BHOH2011
BHOH2228

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
CHIS46
CHIS48
CGLU230
CKMH1276
CHOH2198

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE KMH C 1276
ChainResidue
CGLU14
CHIS46
CHIS48
CSER82
CGLY84
CGLY85
CVAL87
CTHR106
CASN108
CPHE119
CTYR145
CGLU230
CZN301
CHOH2198

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
DHIS46
DHIS48
DGLU230
DKMH1276
DHOH2209

site_idAC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE KMH D 1276
ChainResidue
DGLU14
DHIS46
DHIS48
DSER82
DGLY84
DGLY85
DVAL87
DTHR106
DASN108
DPHE119
DTYR145
DGLU230
DZN301
DHOH2008
DHOH2209

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 1277
ChainResidue
AHOH2013
BHOH2086
BHOH2087
DASP61
DGLU65
DHOH2059

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:21632536, ECO:0007744|PDB:2Y7F
ChainResidueDetails
AGLU14
BASN108
CGLU14
CSER82
CGLY85
CTHR106
CASN108
DGLU14
DSER82
DGLY85
DTHR106
ASER82
DASN108
AGLY85
ATHR106
AASN108
BGLU14
BSER82
BGLY85
BTHR106

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:21632536, ECO:0007744|PDB:2Y7D, ECO:0007744|PDB:2Y7E, ECO:0007744|PDB:2Y7F, ECO:0007744|PDB:2Y7G
ChainResidueDetails
AHIS46
DHIS46
DHIS48
DGLU230
AHIS48
AGLU230
BHIS46
BHIS48
BGLU230
CHIS46
CHIS48
CGLU230

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PDB entries from 2024-10-09

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