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2Y2D

crystal structure of AmpD holoenzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008745molecular_functionN-acetylmuramoyl-L-alanine amidase activity
A0009253biological_processpeptidoglycan catabolic process
A0009254biological_processpeptidoglycan turnover
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0005737cellular_componentcytoplasm
B0008745molecular_functionN-acetylmuramoyl-L-alanine amidase activity
B0009253biological_processpeptidoglycan catabolic process
B0009254biological_processpeptidoglycan turnover
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
C0005737cellular_componentcytoplasm
C0008745molecular_functionN-acetylmuramoyl-L-alanine amidase activity
C0009253biological_processpeptidoglycan catabolic process
C0009254biological_processpeptidoglycan turnover
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
C0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1180
ChainResidue
AHIS34
AHIS154
AASP164
AHOH2273

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1180
ChainResidue
BHIS34
BHIS154
BASP164
BHOH2314

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1180
ChainResidue
CHIS154
CASP164
CHOH2276
CHIS34

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P75820
ChainResidueDetails
AGLU116
BGLU116
CGLU116

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:12654266
ChainResidueDetails
AHIS34
AHIS154
AASP164
BHIS34
BHIS154
BASP164
CHIS34
CHIS154
CASP164

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P75820
ChainResidueDetails
ALYS162
BLYS162
CLYS162

226707

PDB entries from 2024-10-30

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