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1RMQ

Crystal structure of AphA class B acid phosphatase/phosphotransferase with osmiate mimicking the catalytic intermediate

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 CO A 401
ChainResidue
AASP44
AASP46
AASP167
AOS402
AHOH408
AHOH428

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OS A 402
ChainResidue
AASP44
ACO401
AHOH442

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO B 403
ChainResidue
BASP44
BASP46
BASP167
BOS404
BHOH495
BHOH551

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OS B 404
ChainResidue
BASP44
BCO403
BHOH442
BHOH548
BHOH549

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE OS A 405
ChainResidue
AHIS22

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE OS B 406
ChainResidue
BHIS22

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

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PDB entries from 2024-07-24

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