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1L7N

TRANSITION STATE ANALOGUE OF PHOSPHOSERINE PHOSPHATASE (ALUMINUM FLUORIDE COMPLEX)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0006564biological_processL-serine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0016787molecular_functionhydrolase activity
A0036424molecular_functionL-phosphoserine phosphatase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0005737cellular_componentcytoplasm
B0006564biological_processL-serine biosynthetic process
B0008652biological_processamino acid biosynthetic process
B0016787molecular_functionhydrolase activity
B0036424molecular_functionL-phosphoserine phosphatase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ALF B 720
ChainResidue
BASP511
BHOH1008
BPHE512
BASP513
BSER599
BGLY600
BLYS644
BASN670
BMG721
BHOH802

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 721
ChainResidue
BASP511
BASP513
BASP667
BAF3719
BALF720
BHOH877
BHOH1008

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ALF A 220
ChainResidue
AASP11
APHE12
AASP13
ASER99
AGLY100
ALYS144
AASN170
AMG221
AHOH801
AHOH863
AHOH895

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 221
ChainResidue
AASP11
AASP13
AASP167
AAF3219
AALF220
AHOH863
AHOH895

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 300
ChainResidue
AASN48
ALYS140
AGLU141
AHOH813
AHOH929
AHOH993
BLYS504

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AF3 B 719
ChainResidue
BASP511
BPHE512
BASP513
BSER599
BGLY600
BLYS644
BASN670
BMG721
BHOH802
BHOH877
BHOH1008

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AF3 A 219
ChainResidue
AASP11
APHE12
AASP13
ASER99
AGLY100
ALYS144
AASN170
AMG221
AHOH801
AHOH863
AHOH895

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:11342136, ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918
ChainResidueDetails
AASP11
BASP511

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11342136, ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918
ChainResidueDetails
AASP13
BASP513

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:11342136, ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918
ChainResidueDetails
AASP11
BGLU520
BARG556
BSER599
BLYS644
BASP667
AASP13
AGLU20
AARG56
ASER99
ALYS144
AASP167
BASP511
BASP513

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051918
ChainResidueDetails
AASN170
BASN670

Catalytic Information from CSA
site_idCSA1
Number of Residues7
Detailsa catalytic site defined by CSA, PubMed 12051918, 10567362
ChainResidueDetails
AASP13
AASP13
AGLY100
AASP11
ALYS144
AASP171
APHE12

site_idCSA2
Number of Residues7
Detailsa catalytic site defined by CSA, PubMed 12051918, 10567362
ChainResidueDetails
BASP513
BASP513
BLYS644
BASP671
BPHE512
BASP511
BGLY600

site_idMCSA1
Number of Residues6
DetailsM-CSA 727
ChainResidueDetails
ATHR15covalently attached, metal ligand, nucleofuge, nucleophile
ALEU16electrostatic stabiliser
AVAL17metal ligand, proton acceptor, proton donor
ALYS108electrostatic stabiliser
AALA152electrostatic stabiliser
AGLY179electrostatic stabiliser, metal ligand

site_idMCSA2
Number of Residues6
DetailsM-CSA 727
ChainResidueDetails
BTHR515covalently attached, metal ligand, nucleofuge, nucleophile
BLEU516electrostatic stabiliser
BVAL517metal ligand, proton acceptor, proton donor
BLYS608electrostatic stabiliser
BALA652electrostatic stabiliser
BGLY679electrostatic stabiliser, metal ligand

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PDB entries from 2025-06-18

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