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4ODI

2.6 Angstrom Crystal Structure of Putative Phosphoglycerate Mutase 1 from Toxoplasma gondii

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006096biological_processglycolytic process
A0016868molecular_functionintramolecular phosphotransferase activity
B0003824molecular_functioncatalytic activity
B0006096biological_processglycolytic process
B0016868molecular_functionintramolecular phosphotransferase activity
C0003824molecular_functioncatalytic activity
C0006096biological_processglycolytic process
C0016868molecular_functionintramolecular phosphotransferase activity
D0003824molecular_functioncatalytic activity
D0006096biological_processglycolytic process
D0016868molecular_functionintramolecular phosphotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
ATYR155
ALYS156
AVAL158
AASN160
AHOH410

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 301
ChainResidue
BHOH438
BHOH451
BTYR155
BVAL158
BASN160
BLEU163

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA C 301
ChainResidue
CTYR155
CVAL158
CASN160
CLEU163
CHOH417

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA D 301
ChainResidue
DTYR155
DVAL158
DASN160

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsTwN
ChainResidueDetails
ALEU23-ASN32

218853

PDB entries from 2024-04-24

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