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4IQD

Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from Bacillus anthracis

Replaces:  3IH1
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016829molecular_functionlyase activity
A0016833molecular_functionoxo-acid-lyase activity
A0019629biological_processpropionate catabolic process, 2-methylcitrate cycle
A0046421molecular_functionmethylisocitrate lyase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0016829molecular_functionlyase activity
B0016833molecular_functionoxo-acid-lyase activity
B0019629biological_processpropionate catabolic process, 2-methylcitrate cycle
B0046421molecular_functionmethylisocitrate lyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR A 401
ChainResidue
ATYR51
ASER53
AALA55
AASP92
AARG162
APRO240
AVAL241
AHOH515

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR A 402
ChainResidue
ALEU171
AHOH607
AHOH671
BARG166
BLEU171
BGLU199
BHOH589
AGLY170

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR A 403
ChainResidue
ATYR223
ATYR224
AGLU228
ALYS265
AHOH675
BGLU228

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR A 404
ChainResidue
AGLU76
AARG77
AASP80
AHOH506
AHOH594
BGLU76
BARG77
BHOH501

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYR B 401
ChainResidue
BTYR51
BSER53
BALA55
BASP92
BARG162
BILE238
BPRO240
BHOH506
BHOH560

Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KKCGHL
ChainResidueDetails
ALYS127-LEU132

218853

PDB entries from 2024-04-24

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