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6FW2

Crystal Structure of human mARC1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0009253biological_processpeptidoglycan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030151molecular_functionmolybdenum ion binding
A0030170molecular_functionpyridoxal phosphate binding
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue MTE A 1201
ChainResidue
ALYS67
ALEU214
APHE237
AARG238
AASN240
ACYS270
ASER271
ACYS273
ATYR317
AEFK1202
AHOH1359
ASER68
AHOH1426
AHOH1536
AASP91
AARG92
AASP209
ATHR210
ASER211
APRO212
APHE213

site_idAC2
Number of Residues5
Detailsbinding site for residue EFK A 1202
ChainResidue
ASER271
AARG272
ACYS273
ATHR276
AMTE1201

site_idAC3
Number of Residues17
Detailsbinding site for residue B3P A 1203
ChainResidue
AGLU1011
AASP1020
AGLY1030
AHIS1031
ALEU1032
AASP1070
APHE1104
AGLN1105
AARG1145
AHOH1317
AHOH1320
AHOH1340
AHOH1365
AHOH1369
AHOH1398
AHOH1416
AHOH1477

site_idAC4
Number of Residues3
Detailsbinding site for residue MOO A 1204
ChainResidue
AARG1014
ALEU1015
ALYS1016

site_idAC5
Number of Residues7
Detailsbinding site for residue MOO A 1205
ChainResidue
AGLY1113
APHE1114
ATHR1115
AASN1116
ASER1117
AASN1132
AHOH1417

site_idAC6
Number of Residues7
Detailsbinding site for residue MOO A 1206
ChainResidue
AARG188
ATRP1126
AHOH1301
AHOH1304
AHOH1305
AHOH1450
AHOH1458

site_idAC7
Number of Residues7
Detailsbinding site for residue MOO A 1207
ChainResidue
ATHR1142
APRO1143
AASN1144
AARG1145
AHOH1379
AHOH1491
AHOH1506

site_idAC8
Number of Residues4
Detailsbinding site for residue PO4 A 1208
ChainResidue
AARG200
APRO201
ALYS202
AHOH1374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:30397129, ECO:0007744|PDB:6FW2
ChainResidueDetails
ALYS67
ACYS273
ATYR317
ASER68
AARG92
ATHR210
ASER211
AARG238
AASN240
ASER271
AARG272

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP1020

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

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PDB entries from 2024-10-09

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