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1N9K

Crystal structure of the bromide adduct of AphA class B acid phosphatase/phosphotransferase from E. coli at 2.2 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003993molecular_functionacid phosphatase activity
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0036424molecular_functionL-phosphoserine phosphatase activity
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003993molecular_functionacid phosphatase activity
B0016787molecular_functionhydrolase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0036424molecular_functionL-phosphoserine phosphatase activity
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1213
ChainResidue
AASP44
AASP46
AASP167
AHOH1277
AHOH1296
AHOH1395

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1214
ChainResidue
BHOH1293
BHOH1380
BASP44
BASP46
BASP167

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 213
ChainResidue
ALEU196
AHOH1254
BHOH1281

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 214
ChainResidue
ATHR151
ALYS152

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 215
ChainResidue
APHE63
ATYR70
AASN73

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 216
ChainResidue
AASP169
AHOH1269

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 217
ChainResidue
ASER64
APRO65
AGLU66

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 218
ChainResidue
AGLN28
AASN31
AHOH1324

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 219
ChainResidue
AGLN96

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR B 220
ChainResidue
BGLN96

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 221
ChainResidue
BLEU196
BHOH1243

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR B 222
ChainResidue
BGLY144
BTHR151
BLYS152
BHOH1283

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 223
ChainResidue
BASP169
BPRO197
BHOH1278

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 224
ChainResidue
BPHE63
BTYR70
BASN73

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 225
ChainResidue
BSER64
BPRO65
BGLU66

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR B 226
ChainResidue
BPRO116
BALA134
BPHE142
BGLN149

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 227
ChainResidue
BGLY83
BTRP84
BHOH1332

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP44
BASP44

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AASP46
BASP46

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AASP44
BASP167
AASP46
ATHR112
ALYS152
AASP167
BASP44
BASP46
BTHR112
BLYS152

221716

PDB entries from 2024-06-26

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