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3RZZ

Structure of Hydroxyethylphoshphonate Dioxygenase Y98F Mutant

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 Residues6
DetailsBINDING SITE FOR RESIDUE CD A 444
ChainResidue
AHIS129
AGLU176
AHIS182
AHOH555
AHOH563
AHOH574

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 445
ChainResidue
AHOH637
AHOH638
AHIS10
AGLU131
AHOH579

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 446
ChainResidue
AASP142
AHIS160
AHIS163
AHOH517
AHOH558
AHOH639

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 447
ChainResidue
AHIS82
AHOH470
AHOH568
AHOH586
AHOH617
AHOH678

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 448
ChainResidue
AGLN296
ALYS302
AHIS330
AHOH567
AHOH679

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 449
ChainResidue
ACYS180
AASP298
AHOH577
AHOH580
AHOH629

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 450
ChainResidue
AARG340
AASP342
AHOH698

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 451
ChainResidue
AGLU80
AHOH578
AHOH644

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 452
ChainResidue
AASP66
AHOH561
AHOH640
AHOH695

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 453
ChainResidue
AHIS75
AHOH536
AHOH687

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 454
ChainResidue
AHIS94
AARG265
AHOH684
AHOH688

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 455
ChainResidue
AGLU209
AHIS410
AHOH616
AHOH669

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 456
ChainResidue
AASP32
AASP309
AHOH565
AHOH681

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 457
ChainResidue
ACYS180
AHOH593

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 458
ChainResidue
AASP189
AGLU368
AHIS397
AHOH582
AHOH653

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
APHE98
AASN126
AGLU176
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

225158

PDB entries from 2024-09-18

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