Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1K4P

Crystal Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase in complex with zinc ions

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005575cellular_componentcellular_component
A0008686molecular_function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
A0009231biological_processriboflavin biosynthetic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
AARG36
AHOH1174
AHOH1219
AGLU37
ATHR92
AARG150
AGLY152
AHIS153
ATHR154
AZN1004
AHOH1086

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
AGLN81
AARG141
AARG205
AHOH1069
AHOH1091
AHOH1158

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1003
ChainResidue
AGLU181
AGLU183
AHOH1067
AHOH1068
AHOH1069
AHOH1091

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 1004
ChainResidue
AGLU37
AHIS153
ASO41001
AZN1005
AZN1006
AHOH1024
AHOH1219

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1005
ChainResidue
AASP41
AGLU174
AZN1004
AHOH1111
AHOH1219

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1006
ChainResidue
AGLU37
AZN1004
AZN1007
AHOH1073
AHOH1075
AHOH1174

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1007
ChainResidue
ATYR94
AHIS136
AZN1006
AHOH1075
AHOH1161
AHOH1174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11827524, ECO:0007744|PDB:1K4L
ChainResidueDetails
AGLU37
AHIS153

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q5A3V6
ChainResidueDetails
AASP41
ATHR92
AARG150

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Essential for catalytic activity => ECO:0000250
ChainResidueDetails
AHIS136
AGLU174

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: S-glutathionyl cysteine => ECO:0000250|UniProtKB:Q99258
ChainResidueDetails
ACYS66

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1k4l
ChainResidueDetails
AHIS136
AGLU174
AASP99
ATYR94
ACYS66
AASP41

site_idMCSA1
Number of Residues8
DetailsM-CSA 683
ChainResidueDetails
AGLU37metal ligand
AASP41proton acceptor
ACYS66proton donor
ATYR94electrostatic stabiliser
AASP99electrostatic stabiliser
AHIS136electrostatic stabiliser, proton acceptor, proton donor
AHIS153metal ligand
AGLU174proton acceptor, proton donor

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon