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2MAD

THE ACTIVE SITE STRUCTURE OF METHYLAMINE DEHYDROGENASE: HYDRAZINES IDENTIFY C6 AS THE REACTIVE SITE OF THE TRYPTOPHAN DERIVED QUINONE COFACTOR

Replaces:  1MAD
Functional Information from GO Data
ChainGOidnamespacecontents
H0016491molecular_functionoxidoreductase activity
H0030058molecular_functionamine dehydrogenase activity
H0042597cellular_componentperiplasmic space
H0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
L0009308biological_processamine metabolic process
L0016491molecular_functionoxidoreductase activity
L0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
L0030288cellular_componentouter membrane-bounded periplasmic space
L0042597cellular_componentperiplasmic space
L0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
Functional Information from PROSITE/UniProt
site_idPS00583
Number of Residues24
DetailsPFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. AG.AtNKApiDaLSGgrkadtwrpG
ChainResidueDetails
HALA244-GLY267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Tryptophylquinone
ChainResidueDetails
LTRQ57

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Tryptophan tryptophylquinone (Trp-Trp)
ChainResidueDetails
LTRQ57
LTRP108

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bbk
ChainResidueDetails
LASP76
LTHR122
LASP32
LTYR119
LTRP108

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PDB entries from 2024-07-17

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