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1Z2L

Crystal structure of Allantoate-amidohydrolase from E.coli K12 in complex with substrate Allantoate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000256biological_processallantoin catabolic process
A0005737cellular_componentcytoplasm
A0006144biological_processpurine nucleobase metabolic process
A0008270molecular_functionzinc ion binding
A0009442biological_processallantoin assimilation pathway
A0016787molecular_functionhydrolase activity
A0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A0030145molecular_functionmanganese ion binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0047652molecular_functionallantoate deiminase activity
B0000256biological_processallantoin catabolic process
B0005737cellular_componentcytoplasm
B0006144biological_processpurine nucleobase metabolic process
B0008270molecular_functionzinc ion binding
B0009442biological_processallantoin assimilation pathway
B0016787molecular_functionhydrolase activity
B0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B0030145molecular_functionmanganese ion binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0047652molecular_functionallantoate deiminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 511
ChainResidue
AHIS83
AASP94
AHIS192
AZN512
AHOH629
AHOH631

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 512
ChainResidue
AZN511
AHOH631
AASP94
AGLU129
AHIS384

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 513
ChainResidue
BHIS83
BASP94
BHIS192
BZN514
BHOH590
BHOH591

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 514
ChainResidue
BASP94
BGLU129
BGLN195
BHIS384
BZN513
BHOH591

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 513
ChainResidue
AGLN215
AARG217
AARG290
AALA358
AGLY359
BHIS228
B1AL516

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 515
ChainResidue
BGLN215
BARG217
BARG290
BALA358
BGLY359
BHOH534

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 1AL B 516
ChainResidue
AARG217
AARG290
AHIS384
ASO4513
BHIS228
BASN277
BVAL278
BHOH552

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17362992, ECO:0007744|PDB:1Z2L
ChainResidueDetails
AHIS83
AHIS192
AARG217
BHIS83
BHIS192
BARG217

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17362992, ECO:0000305|PubMed:25020232, ECO:0007744|PDB:1Z2L, ECO:0007744|PDB:4PXD
ChainResidueDetails
AASP94
AGLU129
AHIS384
BASP94
BGLU129
BHIS384

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17362992, ECO:0000269|PubMed:25020232, ECO:0007744|PDB:1Z2L, ECO:0007744|PDB:4PXD
ChainResidueDetails
AASN277
AARG290
BASN277
BARG290

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
AGLU128

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
BGLU128

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PDB entries from 2024-07-24

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