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5E6X

Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0007160biological_processcell-matrix adhesion
A0007229biological_processintegrin-mediated signaling pathway
A0008305cellular_componentintegrin complex
A0038023molecular_functionsignaling receptor activity
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CrCdtGyiGKnC
ChainResidueDetails
ACYS448-CYS459

site_idPS00243
Number of Residues14
DetailsINTEGRIN_BETA Integrins beta chain cysteine-rich domain signature. CsGl..GdCvCgqClC
ChainResidueDetails
ACYS484-CYS497

site_idPS01186
Number of Residues14
DetailsEGF_2 EGF-like domain signature 2. CrCdtGYigknce..C
ChainResidueDetails
ACYS448-CYS461

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
ChainResidueDetails
APRO353
ATHR355
AASP451

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72
ChainResidueDetails
AVAL358

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
ChainResidueDetails
ATHR359

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
ChainResidueDetails
AGLN390
AGLY446
ACYS448
ACYS450

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and liganded-open conformation => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEN
ChainResidueDetails
ASER481

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000305|PubMed:2954816
ChainResidueDetails
AGLN1

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN28

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
ChainResidueDetails
AASN94

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
ChainResidueDetails
AASP429

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ALEU471
AASN479

218853

PDB entries from 2024-04-24

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