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4AS3

Pseudomonas Aeruginosa Phosphorylcholine Phosphatase. Orthorhombic form

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0016787molecular_functionhydrolase activity
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
C0016787molecular_functionhydrolase activity
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
D0016787molecular_functionhydrolase activity
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1328
ChainResidue
AASP31
AASP33
AASP262
AHOH2011
AHOH2012
AHOH2015

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1328
ChainResidue
BHOH2013
BHOH2015
BHOH2017
BASP31
BASP33
BASP262

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 1328
ChainResidue
CASP31
CASP33
CASP262
CHOH2009
CHOH2010
CHOH2011

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 1328
ChainResidue
DASP31
DASP33
DASP262
DHOH2019
DHOH2020
DHOH2023

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 1329
ChainResidue
AASP31
AALA167
ALYS242
ASER266
ABTB1330
AHOH2014

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B 1329
ChainResidue
BASP31
BALA167
BLYS242
BSER266
BBTB1330
BHOH2014

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL C 1329
ChainResidue
CASP31
CALA167
CLYS242
CSER266
CBTB1330
CHOH2009
CHOH2010

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL D 1329
ChainResidue
DALA167
DLYS242
DSER266
DBTB1330
DHOH2019
DHOH2022

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BTB A 1330
ChainResidue
AASP40
AGLU43
ATYR95
AALA167
AALA168
ATHR263
ACL1329
AHOH2012
AHOH2014
AHOH2098

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BTB B 1330
ChainResidue
BASP33
BASP40
BGLU42
BGLU43
BTYR95
BALA167
BTHR263
BCL1329
BHOH2015
BHOH2021
BHOH2033

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BTB C 1330
ChainResidue
CASP33
CASP40
CGLU43
CTYR95
CALA167
CTHR263
CCL1329
CBTB1332
CHOH2009

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BTB D 1330
ChainResidue
DASP33
DASP40
DGLU43
DTYR95
DALA167
DTHR263
DCL1329
DHOH2020
DHOH2029

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BTB A 1331
ChainResidue
AASP90
AASP91
AMET239
AASP265
AHOH2115
BTRP233

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BTB B 1331
ChainResidue
BMET239
ALYS211
AALA214
AGLU215
BASP90
BASP91

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BTB C 1331
ChainResidue
CASP90
CASP91
CMET92
CMET239
CHOH2086
CHOH2087
DTRP233

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BTB D 1331
ChainResidue
DASP90
DASP91
DASP132
DASP265

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BTB A 1332
ChainResidue
AGLU43
ATYR84
ACYS87
AGLU88
AHOH2036

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BTB C 1332
ChainResidue
CGLU43
CTYR84
CCYS87
CBTB1330

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:18801468
ChainResidueDetails
AASP31
BASP31
CASP31
DASP31

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:18801468
ChainResidueDetails
AASP33
BASP33
CASP33
DASP33

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:22922065, ECO:0007744|PDB:4AS2, ECO:0007744|PDB:4AS3
ChainResidueDetails
AASP31
DASP31
DASP33
DASP262
AASP33
AASP262
BASP31
BASP33
BASP262
CASP31
CASP33
CASP262

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PDB entries from 2024-07-10

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