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5JEZ

Crystal structure of type 2 PDF from Streptococcus agalactiae in complex with tripeptide Met-Ala-Ser

Functional Information from GO Data
ChainGOidnamespacecontents
A0006412biological_processtranslation
A0016787molecular_functionhydrolase activity
A0018206biological_processpeptidyl-methionine modification
A0042586molecular_functionpeptide deformylase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue ACT A 301
ChainResidue
AHIS145
AGLU158
AASP177
AARG187
AZN306
AHOH444
AHOH472
AHOH618

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 302
ChainResidue
AOCS131
AHIS174
AHIS178
AHOH447
AHOH620
AGLN77

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN A 303
ChainResidue
AHIS55
AGLU198
AHOH488
AHOH557
AHOH642

site_idAC4
Number of Residues7
Detailsbinding site for residue ZN A 304
ChainResidue
AHIS118
AASP154
AHOH421
AHOH622
AHOH624
AHOH644
AHOH654

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN A 305
ChainResidue
AASP94
AGLU190
AHOH484
AHOH527
AHOH556

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN A 306
ChainResidue
AHIS145
AGLU158
AACT301
AHOH627

site_idAC7
Number of Residues6
Detailsbinding site for residue ZN A 307
ChainResidue
AHIS12
AASP18
AHOH418
AHOH424
AHOH436
AHOH626

site_idAC8
Number of Residues3
Detailsbinding site for residue ZN A 308
ChainResidue
AGLU43
AGLU47
AHOH525

site_idAC9
Number of Residues6
Detailsbinding site for residue ZN A 309
ChainResidue
AGLU102
AGLU151
AHOH582
AHOH617
AHOH636
AHOH641

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

224572

PDB entries from 2024-09-04

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