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5ZDN

The complex structure of FomD with CDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0017000biological_processantibiotic biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue CDP A 301
ChainResidue
ALEU54
AMG304
AMG305
AMG305
AHOH409
AHOH410
AHOH412
AHOH419
AHOH419
AHOH421
AHOH426
ATRP68
AHOH426
AHOH427
AHOH441
AHOH441
AHOH444
AHOH447
APHE71
AARG74
ATRP75
AGLN76
ASER77
ALYS142
ALYS146

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
AGLU127
AASP129
AASP143
AHOH421
AHOH438

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 303
ChainResidue
AASN109
AASP125
AASP129
AHOH402
AHOH438
AHOH450

site_idAC4
Number of Residues5
Detailsbinding site for residue MG A 304
ChainResidue
ACDP301
AHOH409
AHOH412
AHOH421
AHOH444

site_idAC5
Number of Residues8
Detailsbinding site for residue MG A 305
ChainResidue
ACDP301
ACDP301
AHOH419
AHOH419
AHOH426
AHOH426
AHOH441
AHOH441

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL A 306
ChainResidue
AARG20
AASP22
ATYR32
AHIS66
ATRP68
AASP125
AHOH409
AHOH414

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"30010320","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30010320","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZDN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30010320","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZDM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ZDN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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