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6NDS

Structure of an HMG-CoA lyase from Acenitobacter baumannii in complex with coenzyme A and 3-methylmalate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004419molecular_functionhydroxymethylglutaryl-CoA lyase activity
A0006552biological_processL-leucine catabolic process
A0016829molecular_functionlyase activity
A0016833molecular_functionoxo-acid-lyase activity
A0046872molecular_functionmetal ion binding
A0046951biological_processketone body biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue COA A 501
ChainResidue
APHE51
AARG115
ACYS240
ACIT502
AHOH652
AHOH652
AHOH683
AHOH722
AVAL52
ASER53
AILE57
AASN84
AGLY87
AARG90
AASN113
AMET114

site_idAC2
Number of Residues12
Detailsbinding site for residue CIT A 502
ChainResidue
AARG16
AASP17
AGLN20
AALA143
AALA177
ATHR179
AHIS207
AHIS209
ACYS240
ACOA501
AZN507
AHOH623

site_idAC3
Number of Residues3
Detailsbinding site for residue ACT A 503
ChainResidue
ATYR223
AGLY263
AHOH653

site_idAC4
Number of Residues6
Detailsbinding site for residue ACT A 504
ChainResidue
AASN184
AGLN187
AARG190
AGLU261
AILE262
AHOH781

site_idAC5
Number of Residues6
Detailsbinding site for residue ACT A 505
ChainResidue
APRO281
AASP287
ATHR288
AALA293
ALYS294
AHOH628

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 506
ChainResidue
ATHR68
AGLY69
AILE70
AHOH655
AHOH659
AHOH711

site_idAC7
Number of Residues5
Detailsbinding site for residue ZN A 507
ChainResidue
AASP17
AHIS207
AHIS209
ACIT502
AHOH623

221051

PDB entries from 2024-06-12

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