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6K38

Crystal structure of BioU (H233A) from Synechocystis sp.PCC6803 conjugated with DAPA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0006520biological_processamino acid metabolic process
A0008483molecular_functiontransaminase activity
A0009102biological_processbiotin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue CWF A 401
ChainResidue
ALYS124
AMET293
AASN296
AHOH571
APHE178
AGLY179
AVAL180
AASP195
ALYS263
ATHR267
ALEU287
ASER292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199
ChainResidueDetails
ALYS124

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000305|PubMed:32042199
ChainResidueDetails
AGLU194

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor and proton acceptor => ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000305|PubMed:32042199
ChainResidueDetails
AHIS198

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199, ECO:0007744|PDB:6K37
ChainResidueDetails
ATYR60
AALA190
AGLY15

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Allysine => ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199
ChainResidueDetails
ALYS124

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PDB entries from 2024-06-12

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