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5W0U

Crystal structure of MBP fused activation-induced cytidine deaminase (AID) in complex with dCMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0006974biological_processDNA damage response
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0030288cellular_componentouter membrane-bounded periplasmic space
A0034219biological_processcarbohydrate transmembrane transport
A0034289biological_processdetection of maltose stimulus
A0042597cellular_componentperiplasmic space
A0042956biological_processmaltodextrin transmembrane transport
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A0071702biological_processorganic substance transport
A1901982molecular_functionmaltose binding
A1990060cellular_componentmaltose transport complex
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0006974biological_processDNA damage response
B0008643biological_processcarbohydrate transport
B0015144molecular_functioncarbohydrate transmembrane transporter activity
B0015768biological_processmaltose transport
B0016020cellular_componentmembrane
B0030288cellular_componentouter membrane-bounded periplasmic space
B0034219biological_processcarbohydrate transmembrane transport
B0034289biological_processdetection of maltose stimulus
B0042597cellular_componentperiplasmic space
B0042956biological_processmaltodextrin transmembrane transport
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
B0055085biological_processtransmembrane transport
B0060326biological_processcell chemotaxis
B0071702biological_processorganic substance transport
B1901982molecular_functionmaltose binding
B1990060cellular_componentmaltose transport complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN B 2001
ChainResidue
BHIS1056
BCYS1087
BCYS1090
BHOH4001

site_idAC2
Number of Residues8
Detailsbinding site for residue DCM B 2002
ChainResidue
BCYS1087
BTYR1114
BHOH4001
BARG1025
BTHR1027
BASN1051
BSER1085
BPRO1086

site_idAC3
Number of Residues5
Detailsbinding site for residue CA B 2003
ChainResidue
BTHR367
BASN368
BALA370
BASP1045
BPHE1046

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL B 2004
ChainResidue
BARG1107
BPHE1109
BLYS1142
BASP1143

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 2001
ChainResidue
AHIS1056
ACYS1087
ACYS1090
AHOH4001

site_idAC6
Number of Residues8
Detailsbinding site for residue DCM A 2002
ChainResidue
AARG1025
ATHR1027
AASN1051
ASER1085
APRO1086
ACYS1087
ATYR1114
AHOH4001

site_idAC7
Number of Residues5
Detailsbinding site for residue CA A 2003
ChainResidue
ATHR367
AASN368
AALA370
AASP1045
APHE1046

Functional Information from PROSITE/UniProt
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
BPRO108-ASN125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0ABF6
ChainResidueDetails
BALA1058
AALA1058

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27258794
ChainResidueDetails
BHIS1056
BCYS1087
BCYS1090
AHIS1056
ACYS1087
ACYS1090

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:16387847
ChainResidueDetails
BTHR1027
ATHR1027

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:16387847, ECO:0000269|PubMed:18722174
ChainResidueDetails
BSER1038
ASER1038

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PDB entries from 2024-05-01

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