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1B6Z

6-PYRUVOYL TETRAHYDROPTERIN SYNTHASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003874molecular_function6-pyruvoyltetrahydropterin synthase activity
A0005739cellular_componentmitochondrion
A0006729biological_processtetrahydrobiopterin biosynthetic process
A0016829molecular_functionlyase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0003874molecular_function6-pyruvoyltetrahydropterin synthase activity
B0005739cellular_componentmitochondrion
B0006729biological_processtetrahydrobiopterin biosynthetic process
B0016829molecular_functionlyase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS23
AHIS48
AHIS50
AGLU133
AHOH469

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BHOH457
BHIS23
BHIS48
BHIS50
BGLU133

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. VVSTteNvAVYIWEN
ChainResidueDetails
AVAL102-ASN116

site_idPS00987
Number of Residues11
DetailsPTPS_1 6-pyruvoyl tetrahydropterin synthase signature 1. CNNpnGHGHNY
ChainResidueDetails
ACYS42-TYR52

site_idPS00988
Number of Residues8
DetailsPTPS_2 6-pyruvoyl tetrahydropterin synthase signature 2. DHKNLDlD
ChainResidueDetails
AASP88-ASP95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ACYS42
BCYS42

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS89
AGLU133
BHIS89
BGLU133

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AHIS23
AHIS48
AHIS50
BHIS23
BHIS48
BHIS50

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q03393
ChainResidueDetails
ASER18
BSER18

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9R1Z7
ChainResidueDetails
ASER27
BSER27

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q03393
ChainResidueDetails
ATYR127
BTYR127

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b66
ChainResidueDetails
ACYS42
AGLU133

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b66
ChainResidueDetails
BCYS42
BGLU133

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b66
ChainResidueDetails
AASP88
AHIS89

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b66
ChainResidueDetails
BASP88
BHIS89

site_idMCSA1
Number of Residues7
DetailsM-CSA 84
ChainResidueDetails
AHIS23metal ligand
ACYS42electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS48metal ligand
AHIS50metal ligand
AASP88activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS89electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU133electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues7
DetailsM-CSA 84
ChainResidueDetails
BHIS23metal ligand
BCYS42electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS48metal ligand
BHIS50metal ligand
BASP88activator, electrostatic stabiliser, hydrogen bond acceptor
BHIS89electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLU133electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-07-10

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