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6BN2

Crystal structure of Acetyl-CoA acetyltransferase from Elizabethkingia anophelis NUHP1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0006635biological_processfatty acid beta-oxidation
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 401
ChainResidue
ATYR182
AALA243
AALA244
AALA246
AVAL344
AHOH507

site_idAC2
Number of Residues8
Detailsbinding site for residue CA A 402
ChainResidue
AHOH576
AHOH676
AHOH676
AHOH828
AHOH828
AGLY331
AGLY331
AHOH576

site_idAC3
Number of Residues8
Detailsbinding site for residue CA A 403
ChainResidue
AHOH685
AHOH685
AHOH773
AHOH773
AHOH841
AHOH841
AHOH876
AHOH876

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 404
ChainResidue
ALYS67
ATHR81
AASN379
AGLY383

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 405
ChainResidue
ATYR167
ATRP287
ATHR290

Functional Information from PROSITE/UniProt
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNKvCASGMkAVmmaaqaV
ChainResidueDetails
AVAL84-VAL102

site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GAAAICNGgGgAsA
ChainResidueDetails
AGLY373-ALA386

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NvnGGaVAlGHPlGsSG
ChainResidueDetails
AASN338-GLY354

219140

PDB entries from 2024-05-01

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