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4N6W

X-Ray Crystal Structure of Citrate-bound PhnZ

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 201
ChainResidue
AASP59
AHIS80
AHIS104
AFLC203
AHOH444

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 202
ChainResidue
AFLC203
AHOH444
AHIS34
AHIS58
AASP59
AASP161

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FLC A 203
ChainResidue
ATYR24
AHIS34
AASP59
AHIS62
AHIS80
AHIS104
ALYS108
ASER126
ATHR129
AGLN133
AARG158
AASP161
AFE201
AFE202
AHOH308
AHOH311
AHOH406
AHOH444

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24706911, ECO:0007744|PDB:4MLM, ECO:0007744|PDB:4MLN
ChainResidueDetails
ATYR24

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24198335, ECO:0007744|PDB:4N71
ChainResidueDetails
AGLU27

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:24198335, ECO:0000269|PubMed:24706911, ECO:0007744|PDB:4MLM, ECO:0007744|PDB:4MLN, ECO:0007744|PDB:4N6W, ECO:0007744|PDB:4N71
ChainResidueDetails
AHIS34
AASP161
AHIS58
AASP59
AHIS62
AHIS80
AHIS104
ALYS108
ASER126
AARG158

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for stereospecificity with the R-enantiomer => ECO:0000269|PubMed:24706911
ChainResidueDetails
AGLU27

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PDB entries from 2024-08-21

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