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5JHU

Potent, Reversible MetAP2 Inhibitors via FBDD

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MN A 501
ChainResidue
AASP262
AHIS331
AGLU364
AGLU459
AMN502
A6KO505
AHOH621

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 502
ChainResidue
AGLU459
AMN501
A6KO505
AHOH621
AASP251
AASP262

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 503
ChainResidue
APHE269
AHOH655
AHOH655

site_idAC4
Number of Residues5
Detailsbinding site for residue DMS A 504
ChainResidue
ATYR383
ALEU429
ALYS433
AHOH702
AHOH840

site_idAC5
Number of Residues13
Detailsbinding site for residue 6KO A 505
ChainResidue
APHE219
AHIS231
AASP251
AASP262
AHIS331
AILE338
AHIS339
AHIS382
ATYR444
AMN501
AMN502
AHOH621
AHOH797

Functional Information from PROSITE/UniProt
site_idPS01202
Number of Residues17
DetailsMAP_2 Methionine aminopeptidase subfamily 2 signature. DIcKIDfGtHISGriiD
ChainResidueDetails
AASP246-ASP262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:16540317
ChainResidueDetails
ATHR254
AALA362

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930, ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258, ECO:0000269|PubMed:17636946
ChainResidueDetails
AASP274
AASN285
AARG354
APHE387

220113

PDB entries from 2024-05-22

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