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1ZCZ

Crystal structure of Phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase (TM1249) from THERMOTOGA MARITIMA at 1.88 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003937molecular_functionIMP cyclohydrolase activity
A0004643molecular_functionphosphoribosylaminoimidazolecarboxamide formyltransferase activity
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
B0003824molecular_functioncatalytic activity
B0003937molecular_functionIMP cyclohydrolase activity
B0004643molecular_functionphosphoribosylaminoimidazolecarboxamide formyltransferase activity
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0016740molecular_functiontransferase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 453
ChainResidue
AVAL350
AGLU351
AALA353
AASP399
AVAL449
AARG451

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 453
ChainResidue
BASP399
BVAL449
BARG451
BVAL350
BGLU351
BALA353

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PG4 A 454
ChainResidue
AGLY157
ALEU160
AALA161
APHE162
ATRP306
AHOH550
AHOH576
AHOH648
BPHE180
BTYR182

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PG4 B 454
ChainResidue
APHE180
ATYR182
BLEU160
BALA161
BPHE162
BTRP306
BHOH514
BHOH594

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PDB entries from 2024-05-01

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