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3ZHC

Structure of the phytase from Citrobacter braakii at 2.3 angstrom resolution.

Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 1412
ChainResidue
BTHR156
BPRO194
BSER195
BHOH2168

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 1411
ChainResidue
AHOH2186
AARG20
APRO22
ATHR23
ATHR215
AGLU218

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 1413
ChainResidue
BARG20
BPRO22
BTHR23
BTHR215
BGLU218
BHOH2211

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 1414
ChainResidue
BGLU167
BASN168
BPHE172
BSER173
BLYS186

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1412
ChainResidue
AASN316
ALEU376
ALYS377
AHOH2252

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 1415
ChainResidue
BTRP40
BVAL42
BHOH2045
BHOH2049
BHOH2283

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT B 1416
ChainResidue
BTRP40
BASP41
BVAL42
BGLN226
BHOH2048
BHOH2052
BHOH2191

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1413
ChainResidue
AGLY238
AGLU239
BGLU98
BALA102

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1414
ChainResidue
APRO43
ALEU44
AHOH2055
AHOH2293

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 1415
ChainResidue
APRO405
AGLU406
BPRO201

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 1418
ChainResidue
BVAL83
BHIS113
BHOH2084
BHOH2106

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 1416
ChainResidue
AMET6
AGLN387
AMET389

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 1417
ChainResidue
ALYS373
AASP375

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 1419
ChainResidue
ALEU47
AGLN91
AHOH2059

site_idBC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT B 1420
ChainResidue
BTHR177

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1421
ChainResidue
BGLN36
BTRP37
BARG264
BHOH2038

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1418
ChainResidue
APHE25
AGLN36
ATRP37

site_idBC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1422
ChainResidue
BGLN257

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1423
ChainResidue
BLYS183
BCYS187
BTHR188
BALA192

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1419
ChainResidue
AASN73
ASER79
AGLN82

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1420
ChainResidue
APRO49
AARG50
AGLN226

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1424
ChainResidue
BPRO49
BARG50
BGLN226

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1425
ChainResidue
BASN126
BPRO127
BVAL128
BARG266

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 1421
ChainResidue
AASN126
APRO127
AVAL128
ALYS129
AARG266

site_idCC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1426
ChainResidue
AASN136
BSER211
BHOH2181

Functional Information from PROSITE/UniProt
site_idPS00616
Number of Residues15
DetailsHIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LerVviVsRHGvRaP
ChainResidueDetails
ALEU8-PRO22

site_idPS00778
Number of Residues17
DetailsHIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. LlFIaGHDTNLanLsgA
ChainResidueDetails
ALEU296-ALA312

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PDB entries from 2024-07-24

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