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5JEX

Crystal structure of type 2 PDF from Streptococcus agalactiae, crystallized in imidazole buffer

Functional Information from GO Data
ChainGOidnamespacecontents
A0006412biological_processtranslation
A0016787molecular_functionhydrolase activity
A0042586molecular_functionpeptide deformylase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue IMD A 301
ChainResidue
AGLU32
AARG147
AVAL148
ALYS163
ALEU164
AZN310
AHOH420
AHOH597
AHOH693

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AGLN77
AOCS131
AHIS174
AHIS178
AHOH421

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN A 303
ChainResidue
AHIS55
AGLU198
AHOH590
AHOH610
AHOH639

site_idAC4
Number of Residues7
Detailsbinding site for residue ZN A 304
ChainResidue
AHIS118
AASP154
AHOH410
AHOH554
AHOH594
AHOH649
AHOH650

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN A 305
ChainResidue
AASP94
AGLU190
AHOH428
AHOH438
AHOH609

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN A 306
ChainResidue
AHIS145
AGLU158
AHOH622
AHOH623
AHOH629

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN A 307
ChainResidue
AHIS12
AASP18
AHOH463
AHOH539

site_idAC8
Number of Residues5
Detailsbinding site for residue ZN A 308
ChainResidue
AGLU43
AGLU47
ALYS155
AHOH525
AHOH601

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN A 309
ChainResidue
AGLU102
AGLU151
AHOH574
AHOH644

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN A 310
ChainResidue
AGLU32
AIMD301
AHOH420
AHOH670

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00163
ChainResidueDetails
AGLU175

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00163
ChainResidueDetails
AOCS131
AHIS174
AHIS178

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PDB entries from 2024-07-31

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