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6ICO

Pseudomonas putida CBB5 NdmA with theophylline

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0009820biological_processalkaloid metabolic process
A0009822biological_processalkaloid catabolic process
A0010277molecular_functionchlorophyllide a oxygenase [overall] activity
A0015995biological_processchlorophyll biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0032451molecular_functiondemethylase activity
A0046872molecular_functionmetal ion binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
A0055114biological_processobsolete oxidation-reduction process
B0005737cellular_componentcytoplasm
B0009820biological_processalkaloid metabolic process
B0009822biological_processalkaloid catabolic process
B0010277molecular_functionchlorophyllide a oxygenase [overall] activity
B0015995biological_processchlorophyll biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0032451molecular_functiondemethylase activity
B0046872molecular_functionmetal ion binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
B0055114biological_processobsolete oxidation-reduction process
C0005737cellular_componentcytoplasm
C0009820biological_processalkaloid metabolic process
C0009822biological_processalkaloid catabolic process
C0010277molecular_functionchlorophyllide a oxygenase [overall] activity
C0015995biological_processchlorophyll biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0032451molecular_functiondemethylase activity
C0046872molecular_functionmetal ion binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
C0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue FES A 400
ChainResidue
ACYS62
AHIS64
AARG65
ACYS81
AHIS84
ATRP86

site_idAC2
Number of Residues4
Detailsbinding site for residue CO A 401
ChainResidue
AHOH698
AHIS173
AHIS178
AASP289

site_idAC3
Number of Residues7
Detailsbinding site for residue TEP A 402
ChainResidue
APHE168
APRO219
ALEU248
AASN282
AVAL285
AHOH551
AHOH601

site_idAC4
Number of Residues6
Detailsbinding site for residue FES B 400
ChainResidue
BCYS62
BHIS64
BARG65
BCYS81
BHIS84
BTRP86

site_idAC5
Number of Residues4
Detailsbinding site for residue CO B 401
ChainResidue
BHIS173
BHIS178
BASP289
BHOH684

site_idAC6
Number of Residues8
Detailsbinding site for residue TEP B 402
ChainResidue
BPHE168
BPRO219
BLEU248
BASN282
BVAL285
BPHE286
BHOH560
BHOH616

site_idAC7
Number of Residues6
Detailsbinding site for residue FES C 400
ChainResidue
CCYS62
CHIS64
CARG65
CCYS81
CHIS84
CTRP86

site_idAC8
Number of Residues4
Detailsbinding site for residue CO C 401
ChainResidue
CHIS173
CHIS178
CASP289
CHOH742

site_idAC9
Number of Residues8
Detailsbinding site for residue TEP C 402
ChainResidue
CPHE168
CPRO219
CLEU248
CPHE281
CASN282
CVAL285
CHOH556
CHOH704

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
ChainResidueDetails
ACYS62
CHIS64
CCYS81
CHIS84
AHIS64
ACYS81
AHIS84
BCYS62
BHIS64
BCYS81
BHIS84
CCYS62

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PDB entries from 2024-05-01

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