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5ZKK

Crystal structure of Phosphoserine phosphatase from Entamoeba histolytica

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
B0003824molecular_functioncatalytic activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue BME A 301
ChainResidue
ACYS23
AGLU79
AHOH421
BPRO81
BBME301

site_idAC2
Number of Residues10
Detailsbinding site for residue PO4 A 302
ChainResidue
AARG57
AGLU79
AHIS146
AGLY147
A144306
AHOH434
AARG8
AHIS9
AASN15
AGLN21

site_idAC3
Number of Residues4
Detailsbinding site for residue PEG A 303
ChainResidue
AASN46
APHE47
AASP48
ATHR140

site_idAC4
Number of Residues2
Detailsbinding site for residue PEG A 304
ChainResidue
AGLY156
AGLY183

site_idAC5
Number of Residues2
Detailsbinding site for residue PEG A 305
ChainResidue
ALYS3
AASN46

site_idAC6
Number of Residues9
Detailsbinding site for residue 144 A 306
ChainResidue
AARG8
APHE90
AGLY147
AALA148
ATYR165
APO4302
AHOH411
AHOH434
AHOH435

site_idAC7
Number of Residues4
Detailsbinding site for residue GOL A 307
ChainResidue
ATHR2
ACYS133
AGLU137
AGLY183

site_idAC8
Number of Residues3
Detailsbinding site for residue PG4 A 308
ChainResidue
AILE60
AGLN63
ALYS64

site_idAC9
Number of Residues3
Detailsbinding site for residue PEG B 302
ChainResidue
BLYS123
BLEU130
BGLY156

site_idAD1
Number of Residues5
Detailsbinding site for residue PEG B 303
ChainResidue
BLYS3
BILE43
BTHR177
BHOH406
BHOH429

site_idAD2
Number of Residues3
Detailsbinding site for residue GOL B 304
ChainResidue
BTHR2
BCYS133
BGLU137

site_idAD3
Number of Residues10
Detailsbinding site for residue PO4 B 305
ChainResidue
BARG8
BHIS9
BASN15
BGLN21
BARG57
BGLU79
BHIS146
BGLY147
BHOH464
BHOH481

site_idAD4
Number of Residues4
Detailsbinding site for residue PG4 B 306
ChainResidue
BILE33
BGLN63
BLYS64
BHOH447

site_idAD5
Number of Residues10
Detailsbinding site for Di-peptide BME B 301 and CYS B 23
ChainResidue
ATHR114
ABME301
BGLN21
BGLY22
BTHR24
BLYS78
BGLU79
BGLU86
BHOH423
BHOH427

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEtEwN
ChainResidueDetails
ALEU6-ASN15

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PDB entries from 2024-07-24

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