Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4YAR

2-Hydroxyethylphosphonate dioxygenase (HEPD) E176H

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0008198molecular_functionferrous iron binding
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0017000biological_processantibiotic biosynthetic process
A0032923biological_processorganic phosphonate biosynthetic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0055114biological_processobsolete oxidation-reduction process
A1901766biological_processphosphinothricin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue CD A 501
ChainResidue
AHIS129
AHIS176
AHIS182
AHOH695
AHOH696
AHOH697
AHOH728

site_idAC2
Number of Residues2
Detailsbinding site for residue CD A 502
ChainResidue
AASP66
AARG107

site_idAC3
Number of Residues1
Detailsbinding site for residue CD A 503
ChainResidue
AHIS75

site_idAC4
Number of Residues5
Detailsbinding site for residue CD A 504
ChainResidue
AHIS10
AGLU131
AACT512
AHOH604
AHOH638

site_idAC5
Number of Residues6
Detailsbinding site for residue CD A 505
ChainResidue
AASP32
AASP309
AHOH601
AHOH611
AHOH624
AHOH641

site_idAC6
Number of Residues4
Detailsbinding site for residue CD A 506
ChainResidue
AHIS94
AHOH670
AHOH705
AHOH711

site_idAC7
Number of Residues5
Detailsbinding site for residue CD A 507
ChainResidue
AASP142
AHIS160
AHIS163
AACT513
AHOH803

site_idAC8
Number of Residues2
Detailsbinding site for residue CD A 508
ChainResidue
AASP189
ACD510

site_idAC9
Number of Residues2
Detailsbinding site for residue CD A 509
ChainResidue
AGLU80
AHOH802

site_idAD1
Number of Residues4
Detailsbinding site for residue CD A 510
ChainResidue
AASP189
AGLU368
AHIS397
ACD508

site_idAD2
Number of Residues6
Detailsbinding site for residue NA A 511
ChainResidue
AGLN296
AHIS330
AHOH605
AHOH702
AHOH783
AHOH806

site_idAD3
Number of Residues7
Detailsbinding site for residue ACT A 512
ChainResidue
AHIS10
AASN13
ALEU130
AGLU131
ATYR179
ACD504
AHOH604

site_idAD4
Number of Residues6
Detailsbinding site for residue ACT A 513
ChainResidue
AASP142
AHIS160
AHIS163
AASP373
ACD507
AHOH803

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues39
DetailsDNA_BIND: H-T-H motif => ECO:0000250
ChainResidueDetails
AALA19-GLY38
ATHR245-ARG265

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:3GBF
ChainResidueDetails
ALYS16

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: in other chain => ECO:0007744|PDB:3GBF
ChainResidueDetails
ATYR98
AASN126
AHIS176
AHIS182
ASER196

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19516340, ECO:0000269|PubMed:21711001, ECO:0007744|PDB:3G7D, ECO:0007744|PDB:3GBF, ECO:0007744|PDB:3RZZ
ChainResidueDetails
AHIS129

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon