Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2RBT

n-methylbenzylamine in complex with Cytochrome C Peroxidase W191G

Functional Information from GO Data
ChainGOidnamespacecontents
X0004601molecular_functionperoxidase activity
X0006979biological_processresponse to oxidative stress
X0020037molecular_functionheme binding
X0034599biological_processcellular response to oxidative stress
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 X 1001
ChainResidue
XTYR36
XASP37
XHIS181

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM X 400
ChainResidue
XLEU171
XMET172
XALA174
XHIS175
XLEU177
XGLY178
XLYS179
XTHR180
XHIS181
XASN184
XSER185
XLEU232
XTHR234
XHOH4016
XHOH4024
XHOH4038
XHOH4162
XPRO44
XARG48
XTRP51
XPRO145
XASP146
XALA147

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 271 X 4001
ChainResidue
XHIS175
XLEU177
XLYS179
XTHR180
XGLY191
XPHE202
XMET230
XMET231
XASP235

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD X 2001
ChainResidue
XASP148
XSER185
XTYR187
XASN220
XHOH4246

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MPD X 3001
ChainResidue
XLEU30
XARG31
XGLU118
XMET119
XASN196
XHOH4034
XHOH4061
XHOH4100
XHOH4135
XHOH4201
XHOH4262
XHOH4332

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVALMGAHAL
ChainResidueDetails
XGLU167-LEU177

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GPvlVRLaWHIS
ChainResidueDetails
XGLY43-SER54

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
XHIS52

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Tryptophan radical intermediate => ECO:0000269|PubMed:2851317
ChainResidueDetails
XGLY191

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:10722697, ECO:0000269|PubMed:11170452, ECO:0000269|PubMed:2169873, ECO:0000269|PubMed:6092361, ECO:0000269|PubMed:8384877, ECO:0000269|PubMed:8673607
ChainResidueDetails
XHIS175

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
XARG48

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18407956
ChainResidueDetails
XTYR153

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
XARG48
XHIS52
XASN82

site_idMCSA1
Number of Residues3
DetailsM-CSA 709
ChainResidueDetails
XARG48electrostatic stabiliser
XHIS52electrostatic stabiliser, proton acceptor, proton donor
XGLY191single electron acceptor, single electron donor

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon