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2HXC

Crystal structure of the benzylamine complex of aromatic amine dehydrogenase in N-semiquinone form

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0030058molecular_functionamine dehydrogenase activity
A0030059molecular_functionaralkylamine dehydrogenase (azurin) activity
A0042597cellular_componentperiplasmic space
B0016491molecular_functionoxidoreductase activity
B0030058molecular_functionamine dehydrogenase activity
B0030059molecular_functionaralkylamine dehydrogenase (azurin) activity
B0042597cellular_componentperiplasmic space
D0009308biological_processamine metabolic process
D0016491molecular_functionoxidoreductase activity
D0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
D0030059molecular_functionaralkylamine dehydrogenase (azurin) activity
D0042597cellular_componentperiplasmic space
H0009308biological_processamine metabolic process
H0016491molecular_functionoxidoreductase activity
H0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
H0030059molecular_functionaralkylamine dehydrogenase (azurin) activity
H0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ABN D 1369
ChainResidue
DASP84
DTTQ109
DASP128
DASN156
DVAL158
DASN159
DPHE169
DHOH1481

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ABN D 1370
ChainResidue
DASP84
DTTQ109
DASN156
DVAL158
DASN159
DHOH1481
BLEU100

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ABN H 1301
ChainResidue
ALEU100
HASP84
HTTQ109
HASN156
HVAL158
HASN159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503
ChainResidueDetails
APHE97
ALEU100
AASN124
BPHE97
BLEU100
BASN124

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560
ChainResidueDetails
DASP128
HASP128

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560
ChainResidueDetails
DASP84
DASN156
HASP84
HASN156

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
DTHR172
HTHR172

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Tryptophylquinone => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503
ChainResidueDetails
DTTQ109
HTTQ109

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503
ChainResidueDetails
DTTQ109
DTRP160
HTTQ109
HTRP160

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bbk
ChainResidueDetails
DTHR172
DASP84
DPHE169
DTRP160
DASP128

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bbk
ChainResidueDetails
HTHR172
HASP84
HPHE169
HTRP160
HASP128

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PDB entries from 2024-07-17

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