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4MLN

Crystal of PhnZ bound to (R)-2-amino-1-hydroxyethylphosphonic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0016491molecular_functionoxidoreductase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 201
ChainResidue
AHIS34
AHIS58
AASP59
AASP161
AHOH301
AHOH347

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 202
ChainResidue
AODV203
AHOH301
AASP59
AHIS80
AHIS104

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ODV A 203
ChainResidue
AGLU27
AASP59
AHIS62
AHIS80
AHIS104
ALYS108
ASER126
ATHR129
AGLN133
AARG158
AFE202
AHOH301
AHOH331
AHOH347
AHOH348

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE B 201
ChainResidue
BTYR24
BHIS34
BHIS58
BASP59
BASP161
BHOH301

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 202
ChainResidue
BASP59
BHIS80
BHIS104
BODV203
BHOH301

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ODV B 203
ChainResidue
BTYR24
BASP59
BHIS62
BHIS80
BHIS104
BVAL105
BLYS108
BSER126
BTHR129
BGLN133
BARG158
BFE202
BHOH301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:24706911, ECO:0007744|PDB:4MLM, ECO:0007744|PDB:4MLN
ChainResidueDetails
ATYR24
BTYR24

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:24198335, ECO:0007744|PDB:4N71
ChainResidueDetails
AGLU27
BGLU27

site_idSWS_FT_FI3
Number of Residues20
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
BHIS34
BHIS58
BASP59
BHIS62
BHIS80
BHIS104
BLYS108
BSER126
BARG158
AHIS58
BASP161
AASP59
AHIS62
AHIS80
AHIS104
ALYS108
ASER126
AARG158

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for stereospecificity with the R-enantiomer => ECO:0000269|PubMed:24706911
ChainResidueDetails
AGLU27
BGLU27

222624

PDB entries from 2024-07-17

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