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2Y2B

crystal structure of AmpD in complex with reaction products

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 Residues13
DetailsBINDING SITE FOR RESIDUE AH0 A 1000
ChainResidue
AHIS34
ALYS162
AASP164
AMHI202
AZN203
AASN35
AILE36
ALEU38
ALEU51
ATYR63
AILE67
AGLU116
AHIS154

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE MHI A 1001
ChainResidue
AHIS34
APHE52
AARG71
AVAL72
ASER73
ATRP95
AHIS96
AALA97
AGLY98
AARG107
AASN109
AGLU116
AHIS154
AARG161
AARG175
AAH0201
AZN203
AHOH414
AHOH424
AHOH311

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1180
ChainResidue
AHIS34
AHIS154
AASP164
AAH0201
AMHI202

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1180
ChainResidue
BHIS34
BHIS154
BASP164
BHOH450

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1180
ChainResidue
CHIS34
CHIS154
CASP164
CHOH430

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

218853

PDB entries from 2024-04-24

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